Professional Documents
Culture Documents
By H. H. Mitchell Richard J. Block (From of Animal Tha York) 13, 1946)
By H. H. Mitchell Richard J. Block (From of Animal Tha York) 13, 1946)
RELATIONSHIPS
TENTS OF PROTEINS
BETWEEN
THE AMINO
AND THEIR
NUTRITIVE
FOR THE RAT
BY H. H. MITCHELL
(From the Division
of Animal
Department
College,
AND
RICHARD
ACID
CONVALUES
J. BLOCK
Nutrition,
University
of Illinois,
and Biochemistry,
New York
and Fifth AvenueHospitals,
New
Urbana,
Aledical
of Physiology
Flower
and tha
York)
600
AMINO
ACIDS
IN
PROTEINS
1 The recent
communication
of Vickery
and Clarke
(5)) criticizing
the method
used
by Block and Boiling
of computing
the amino acid content
of proteins
to a uniform
protein
content
of 16 per cent nitrogen,
expresses
the viewpoint
of the protein
chemist
concerned
solely with problems
of protein
structure.
The viewpoint
of the protein
nutritionist,
however,
is entirely
different,
because the utilization
of dietary
proteins
by animals
can be studied
only by the nitrogen
balance
sheet method
at the present
time.
Hence,
an amino acid analysis
of a protein
is most useful in protein
nutrition
as a chemical
description
of the nitrogen
contained
in it.
From
this standpoint,
it
is entirely
immaterial
whether
the protein
contains
15 or 18 per cent of nitrogen;
in
fact, for the most exact appraisal
of a protein
in nutrition,
such differences
in nitrogen
content
should be disregarded
by computing
amino
acid contents
on a conventional
basis of 16 per cent of nitrogen.
2 A somewhat
similar
use of the amino acid content
of whole egg proteins
has been
made by Stare, Hegsted,
and McKibbin
(11).
a Dried
and solvent-extracted
at low temperatures
by the VioBin
Corporation,
Monticello,
Illinois,
through
the courtesy
of Mr. Ezra Levin.
cently assembled by Block and Bolling (4),l and later discussed by them (6),
from the standpoint of nutritional
applications.
These values have been
revised and supplemented to some extent by more recent analyses.
The
relative amino acid deficiencies of food proteins in the nutrition of the growing rat can be revealed clearly only by a comparison of the proportions
of
the essential amino acids present in the proteins with the proportions existing among the amino acid requirements
of the rat for growth.
These at
present are unknown.
However, in the proteins of whole egg we have an
amino acid mixture that is very highly digestible and almost perfectly
utili.zable in rodent metabolism, being better than milk proteins in this
respect.
This was first shown by Mitchell and Carman (7) for the growing
rat and was later confirmed by Sumner (8) for both growing and mature
rats.
For the adult human subject, also, whole egg proteins seem to be
better utilized than whole milk proteins (9,10).
In Table I are given the percentage deviations of the contents of different
food proteins in the essential amino acids, in Roses sense of the term, and
also in tyrosine and cystine, from the contents of the corresponding
amino
acids found in whole egg protein.2
The first column of the values represents
the results of a recent analysis of a dried preparation of whole egg performed
by one of the authors (R. J. B.).3 The methods used in this analysis will be
given later.
Each value in the other columns expresses the percentage
deviation in the amino acid content of a specified protein mixture (standardized to a nitrogen content of 16 per cent) from that of the proteins of
dried whole egg. For example, beef muscle proteins, according to available
analyses, contain 46 per cent less cystine than whole egg proteins, and 12
per cent more lysine.
The amino acid limiting the nutritional
value for
maintenance and growth of the laboratory rat for any particular food protein would be that amino acid present in the least amount with reference to
acid
Arginine
Histidine
Lysine
Tyrosine
Phenylalanine
Tryptophane
Cystine
Methionine
Cystine +
methionine
Threonine
Leucine
Isoleucine
Valine
Indicated
limiting
amino acid
Amino
-11
+14
-31
-7
+2
-7
$21
+34
+29
4.9 -22
9.2 +2
8.0 -11
7.3
0
LYsine
6.4
2.1
7.2
4.5
6.3
1.5
2.4
4.1
6.5
-Per
cent
Percentage Deviations
-34
+43
+10
+53
-11
-20
-87
-15
-42
Casein
-16
+8
+23
-19
+6
-8
+15
,
,Cystine
Cystine
+ meth - + meth
ionine
ionine
-8
$4
+I8
-10
+7
-58
-17
-32
+24
-33
Cows milk
+10
+13
-20
-12
Methiqnine
$71
-34
+5
$67
+3:
-2
-14
-39
actalbumin
Percentage
-
Methionine
+a
-6
+7
-6
+1!
-11
+fl
$42
-46
-14
-33
$33
-_
+29
+96
-62
-18
Isoleu.
tine
Isoleucine
+22
-79 to -9:
+27
+f38
0
-25 to 4:
-56 -81
+22
-14
+13
+54
-54
-14
+25
-45
A
k262
for whole
Hemoglobin
values
-47
$20
+4s
+33
-6
Blood
senlm
from corresponding
Iuman mill c
deviations
-6
-13
-30
-27
Cystine
+ meth
ionine
-4
-9
-35
-14
Isoleu
tine
-6
-16
-21
-21
Cystine
+ meth.
ionine
-24
-22
-13
-46
-20
-29
-2
+29
-24
+7
-13
+13
-37
-34
-35
+16
+20
+38
+12
+3
-2
-19
-7
-50
-22
-32
+29
Kidney
Heart
Beef muscle
egg proteins
-3
-7
-42
-22
-29
+3
$48
-7
+2
Liver
-2
-9
-30
-15
Isoleutine
._
TABLE
I
of Amino Acid Contents of Food Proteins from Amino Acid Contents of Proteins of Whole Egg Taken
As Standard
s
8
w
2
?
9
i
E!
fj
Et
.x
arid
Arginine
............................
Histidine
...........................
Lysine .............................
Tyrosine
...........................
Phenylalanine
......................
.......................
Tryptophane
............................
Cystine
Methioninc
.........................
Cystine
f- methionine
..............
Threonine
..........................
............................
Leucine
.........................
Isoleucine
Valine ..............................
Indicated
limiting
amino acid.
Amino
......
-__
6.4
2.1
7.2
4.5
6.3
1.5
2.4
4.1
G.5
4.9
9.2
8.0
7.3
fit?7 ten
Whole
egg
proteir
-63
-29
+8
-13
-17
-49
-37
-39
-46
-58
-49
I,ysine
+lf3
$24
+4
-24
-50
-4
Lysine
-21
-44
-35
$31
-29
-65
+13
-11
0
Flax seed
.-
-46
-24
-32
-27
-18
-40
-30
Lysine
+32
+27
+44
-28
-61
-4
-19
-47
-42
-14
-13
-46
-17
-28
-18
-33
-35
-29
Lysine
+x3
imflower
seed
deviations
I-Continued
Percentage
TABLE
0
-58
-2
-14
-33
-33
-51 to -76
-45 -60
-69
-24
-62
+I0
Methionine
+55
Peanut
from corresponding
-19
-9
-10
-20
-21
-51
-40
-18
-28
-41
-42
Methionint
-24
-53
-50
-76
-66
-20
-30
-49
-45
Methioninr
+39
-43
-31
$11
+10
egg proteins
Pea
for whole
Soy bean
values
-29
f7
-33
-44
-40
-33
-28
-55
-40
Isoleucine
+27
-32
-33
Alfalfa
acid
Arginine. ..............
Histidine. .............
Lysine.................
Tyrosine ...............
Ihenylalsnine.
.........
Tryptophsne.
..........
Cystine ................
Methionine ............
Cystine + methionine.
Threonine. .............
Leucine. ...............
Isoleucine......................
Valine. ........................
Indicated limiting amino acid
Amino
6.4
2.1
7.2
4.5
6.3
1.5
2.4
4.1
6.5
4.9
9.2
s.0
7.3
ier ten
Whole
wz
mteir
-86
-59
-G6
-79
-62
- 100
-96
-so
-57
-19
-84
-67
$36
Gelatin
I3yptophane
-~
sinr
LY-
-63
-2
-10
-20
-25
-39
-34
-33
-26
-55
-3s
-34
- 44
Isoleucine
sint
Ly-
-54
-42
-1s
+5
-72
-16
-13
-33
-21
-63
-4s
-45
-24
-16
-33
-33
-67
-51
-57
-22
-27
-G2
-39
White
flour
-6
germ
from
+19
Wheat
___-
____
deviations
I-Coduded
Percentage
TABLE
LYsin6
-24
-130
-50
-32
-29
-21
-47
-37
-24
+a2
-25
-5
-72
corresponding
-50
-1s
Methionine
-13
-13
-25
-61
-4s
-4
A-41
-19
$49
$38
+24
4-6
sine
-14
LY-
-13
-42
-17
-26
-16
-2
-34
yeast
-20
-26
-32
+12
-54
-55
-5s
-33
$33
$4
-20
-35
-13
Average
Cystine +
LYsine: methionine
-30
-14
-29
-10
+5
-20
-25
-41
-35
+2
-29
-56
-6
+5
-54
$13
$27
2&d
oats
egg proteins
White
rice
for whole
Corn germ
values
604
AMINO
ACIDS
IN
PROTEINS
whole egg proteins; i. e., that amino acid with the greatest percentage deficit
in Table I. Thus, the limiting amino acid in pea proteins is methionine
(-76),
that in blood serum proteins isoleucine (-62),
and in wheat proteins lysine ( - 63).
The indicated limiting amino acids listed at the bottom of Table I are
taken to be those essential amino acids in greatest percentage deficit.
In
such deductions, the arginine percentages are disregarded, since the growing rat can, to some unknown extent, supplement a dietary deficiency in
this amino acid by its limited capacity to synthesize it. In view of the
known relationship
of cystine and methionine in metabolism,
whereby
methionine is convertible into cystine but the reverse reaction does not
occur, the limiting factor between these two was assumed to be methionine,
or methionine plus cystine, whichever
percentage deficit is the greater.
The latter designation means that the protein in question is supplemented
fully by methionine and to some extent by cystine also. The same relationship exists between tyrosine and phenylalanine, but the necessity of
distinguishing
between these amino acids in this connection has not arisen
in the construction
of Table I.
The extent to which food proteins will supplement each other in a diet or
ration will depend upon the identity or non-identity
of their limiting amino
acids, and, if they are not identical, upon the relative prominence of a common deficiency in some other essential amino acid. Thus, whole milk proteins should obviously supplement rice proteins because the limiting amino
acid in the one case is cystine plus methionine and in the other case lysine,
but the extent of supplementation
would presumably be slight because rice
proteins are also rather seriously deficient in the sulfur-containing
amino
acids.
Such uses of the values listed in Table I should be tempered by the fact
that several methods of amino acid analysis are still quite imperfect.
The main purpose of presenting the data summarized in Table I is to
compare the amino acid contents of food proteins with reference to the contents in whole egg proteins, with the results of rat feeding experiments designed to detect the limiting amino acids in the same food proteins.
The
largest percentage deficits in essential amino acids for the various food proteins considered in Table I are in harmony with the following conclusions
as to the amino acids limiting the growth-promoting
values of the proteins
for the rat.
The proteins of whole milk (12), beef (13), soy beans (13-15), the peanut
(16,17), yeast (X3), the pea (19), and casein (20,21) are deficient in cystine
or methionine or both.
On the other hand, lactalbumin is definitely not
deficient in cystine (21).
The proteins of wheat (13), oats (13), rye (22), corn (13,23), rice (24), and
H.
H.
MITCHELL
AND
R.
J.
BLOCK
605
606
AMINO
ACIDS
IN
PROTEINS
Value
oj Blood
Whole
egg.
II
Proteins
Constitution
As Revealed
Percentage
6.4
2.1
7.2
4.5
6.3
1.5
2.4
4.1
6.5
4.9
9.2
8.0
7.3
-5
+48
+33
+20
-14
+13
+54
-54
-14
+29
+96
-62
-18
Isoleutine
62
krum
deviation
albumin
-6
by Their
Amino
from whole
Fibrin
y-Globulin
._
+29
-25
+19
-7
+51
-5
+127
-21
-24
-23
f93
+29
-73
-35
+29
+44
+I8
+22
-80
+171
-68
1-5
+4
+29
-75
-4
Tryptophane
80
egg values
+22
+67
+22
Acid
+61
+52
-37
-18
Isoleutine
37
-12
-59
f38
Methionine
73
Relative
H.
H.
MITCHELL
AND
R.
J.
607
BLOCK
column are taken directly from Table I. The biological values and digestibilities of protein, occupying the next two columns, are taken from published and unpublished data secured in the Division of Animal Nutrition
of the University
of Illinois, except for lactalbumin, rice, sesame seed, and
TABLE
Relation
between Percentage
to Whole Egg
Protein
sounx
Deficits
Proteins,
III
in Limiting
Essential
Amino
Acids
and Biological
Values
of Proteins
with
Reference
7-
Limiting
essential
amino
3iolog
ical
value
acid
1Biblioe:raphic
Xges-
reference
NO.
ibility
liver. .........
Egg albumin
.......
Cows milk .........
Lactalbumin .......
Beef kidney
........
I
heart ..........
Casein .............
Sunflower
seed. ....
Soy bean. ..........
Rolled
oats. .......
Yeast,
average.
....
White
rice. ........
Corn germ .........
Sesame seed ........
Wheat
germ ........
Whole wheat .......
Cottonseed.
........
Whole corn .........
White
flour. ........
Peanut.
............
Pea. ...............
Gelatin
............
Cystine
Isoleucine
Lysine
Cystine
Met.hionine
Cystine
Isoleucine
Cystine
Lysine
Methionine
Lysine
Cystine
Lysine
Methionine
Lysine
Isoleucine
Lysine
Methionine
Tryptophane
+ methionine
+ methionine
+ methionine
+ methionine
+ methionine
29
30
31
32
34
35
35
42
47
51
54
55
56
61
61
62
63
63
72
72
76
76
100
:7 cent
76
77
82
90
84
77
74
73
65
75*
66
69
66
78
71
75
70
61
60
52
58
48
100
97
100
95
98
99
100
99
94
96*
93
93
78
85
92
95
91
90
94
100
97
91
25$
951
(35)
(36)
(7)
(12)
(21)
(36)
(36)
C-30)
(37)
(37)
i
(38)
(3%
(40)
!A)
CL)
(7)
(35)
(43)
(44)
* The biological
data were secured
with heated
soy flour.
t The digestibilities
and biological
values given are from unpublished
data secured
on growing
rats in the Division
of Animal
Nutrition,
University
of Illinois.
$ The biological
data were secured
with pork
cracklings
consisting
essentially
of connective
tissue.
the pea. The literature references in the last column of Table III denote
the source of the biological data.
Inspection of Table III reveals a correlation between the chemical and
the biological evaluations of food proteins in that the lower biological values
-IP er ce*i
608
AMINO
ACIDS
IN
PROTEINS
tend to gravitate toward the foot of the table, while the better proteins are
found at the top.
The correlation coetlicient of percentage deficits in limiting essential
amino acids and biological values is -0.861
by the product-moment
method, in which perfect negative correlation is represented by -1.000.
It is worthy of note that little or no correlation exists between amino acid
deficits and coefficients of digestibility,
with r = -0.366.
If the latter
correlation is a significant one, it exists, not because of any inherent relationship between the content of proteins in essential amino acids and their
FIG. 1. Correlation
of proteins.
between
the chemical
constitution
values
Y=biological value
My = 68.3
6y= 13.4
X=%, amino acid deficit
Mx= 53.8
6x= 18.2
= -0.861
H.
H.
MITCHELL
AND
R.
J.
BLOCK
609
100, the difference between 102 and 100 being an error of random sampling.
For a percentage deficit of 100, the biological value should be 39. It seems
reasonable to qualify this latter statement to apply only to proteinswhose
biological efficiency is limited by the complete absence of an amino acid
essential for growth but not for maintenance, such as histidine.
Otherwise, the replacement of endogenous losses is impaired, as well as the ability
to support growth, so that the biological value possesses a somewhat different significance.
With gelatin, tryptophane,
the first limiting amino
acid, is required for maintenance as well as for growth, and the biological
value of 25 is for this reason, perhaps, somewhat less than the prediction, 39.
Hegsted, Hay, and Stare (29) compared the growth-promoting
value of
serum albumin, fibrin, and y-globulin from human plasma with young rats
fed ad libitum in rations containing 20 per cent of protein.
The albumin
proved to be the poorest, the fibrin definitely and markedly the best, almost
as good as the proteins of skim milk powder, and y-globulin was of intermediate value.
The maximum percentage deficits in essential amino acids
for these proteins, given on the bottom line of Table II, agree with this
biological evaluation, the deficits being 37 for fibrin, not much more than
the 32 for milk proteins given in Table III, 73 for y-globulin, and 80 for
albumin.
There are obvious imperfections
in the correlation of chemical and biological data summarized in Table III.
These imperfections may in part be
traceable ultimately to inaccuracies in the data. The average biological
values determined in the Nutrition Laboratory of the University
of Illinois
will have a standard error of about 1.2 (35). The percentage deficits in
limiting amino acids, being difference values, may be subject to a much
greater error.
But there are other disturbing factors in the picture.
The
biological values relate to the total nitrogen content of the food material,
while the amino acid analyses may not. In Table III the animal tissues,
muscle, liver, kidney, and heart, rank higher on the chemical scale than on
the biological scale. All of these tissues contain considerable amounts of
non-protein nitrogenous substances possessing little value in relation to the
animal functions that dietary protein serves.
The biological values of the
true proteins in these tissues may be appreciably higher than those of the
conventional proteins (N X 6.25).
Wheat germ and corn germ proteins, on the other hand, are rated much
lower on the basis of their chemical structure than on that of their biological
performance.
The explanation is not at all obvious.
The high nutritive
value for peanut protein that has been secured by another method of biological assay than the biological value in the sense of Thomas (46) finds no
support from the chemical data reported in Table I.
Another possibility is that an imperfect correlation actually describes the
610
AMINO
ACIDS
IN
PROTEINS
original
dat,a presented
in this section
mere secured
by General
Mills,
Inc., of Minneapolis,
Minnesota.
with
COD.-
H.
H.
MITCHELL
AND
R.
J.
611
BLOCK
Differences
Digestibility
Cereal mixture,
unprocessed TS.
pelleted
Cereal mixture pell ted TS. fully processed
Cereal mixture, unprocessed US. raw
rolled oats
Rolled oats, raw cs. cooked
2.E+4 rt 0.74
3.58
0.72
with
standad
errors
Biological
value
0.42
0.74
11.47
1.23
0.63
0.71
2.10
0.73
1.63
0.68
2.86
1.00
Such an analysis reveals that the pelleting of the cereal mixture definitely depressed the digestibility of the protein, without appreciably affecting its biological value. Further processing, involving treatment under
high steam pressure (gun explosion), definitely and considerably lowered
both the digestibility
and the biological value of the protein.
The ralv
rolled oats contained protein definitely, if only slightly, superior in biological value to t,he protein of the oat-corn-rye
mixture, though no more
digest,ible.
Cooking the rolled oats in accordance with the recommended
domestic practice probably lowers the digestibility
of the protein, and
increases slightly the biological value.
6Puffed oat cereal No. 1.
612
AMINO
ACIDS
IN
PROTEINS
The data reported in Tables V, VI, and VII were obtained with growing
rats in a succession of three experimental periods, the standardizing
period
IV
TABLE
True
Digestibility
and Biological
Value
of Nitrogen
of Cereal
Products
before
and after
Rats*
-7
I
t
Products
True digestibility
Biological value
per cent
12
12
24
30
24
91.67
88.83
85.25
92.30
90.67
f
f
f
f
f
per cent
0.56
0.49
0.53
0.43
0.53
62.67
62.25
50.78$
64.77
67.63
f
-f
*
f
f
0.48
0.56
1.10
0.55
0.83
* These determinations
were carried
Mills, Inc., by Miss Claire A. Frederick
t Puffed oat cereal No. 1.
t Average of eighteen determinations.
TABLE
True
Digestibility
Wheat
Rat No.
Period No.
I_-
Processed mixture*
True
digestibility
per
95
97
99
101
103
96
98
100
102
104
M.
F.
M.
((
F.
Averages
and Biological
Value for Growing
Rats
Flour Mixture
before and after Heat Processing
1
1
1
1
1
3
3
3
3
3
_-
. ... . .. .
cent
86
83
87
88
85
83
83
84
80
82
34.1
-i-
Bi;&&cal
_-
Period No.
-per cent
- _
-
53
50
53
53
51
53
51
53
49
52
51.8
of Nitrogen
i-
Unprocessed mixture
True
digestibility
per cent
3
3
3
3
3
1
1
1
-_
-
1
1
of Oat-Malted
(( Sun Explosion)
Bi&$al
ger cent
90
64
91
94
91
94
91
92
92
94
90
64
65
65
70
70
64
70
64
59
91.9
65.5
being the second, while the first and third periods were planned so that each
rat received each of the test foods, half of them in one order and half in the
reverse order (for further details of the procedure, see (37)).
pelleted. . . . . . . . .
t fully processed.
Rolled oats, raw. . . .
.. .. .. ... ... ..
cooked.
. . .. . .. ... ..
H.
H.
MITCHELL
AND
TABLE
True
Digestibility
Rat No.
and Biological
Oat-Malted
Wheat
Period No.
_M.
F.
M.
F.
_1
1
1
1
1
3
3
3
3
3
*Puffed
oat
True
digestibility
cereal
VI
Digestibility
Rat No.
.-
51
48
50
48
45
52
50
54
55
56
__
50.9
per
Averages
* Puffed
1
1
1
1
1
1
3
3
3
3
3
3
... ... .. . .
oat cereal
No.
3
3
3
3
3
1
1
1
1
1
__
-
90
91
93
94
97
91
94
91
91
97
per cent
--
92.9
69
65
70
68
73
65
67
67
58
58
66.0
VII
1.
cent
Rats of Nitrogen
Mixture*
Rolled oats
True
M.
F.
M.
F.
M.
Bi;&&cal
digestibility
per cent
digestibility
115
117
119
121
123
125
116
118
120
122
124
126
2.
and Biological
Rolled Oats
Period No.
Rolled oats
per cent
TABLE
True
Period No.
True
86.8
No.
of Processed
Rats of Nitrogen
and of Rolled Oats
Mixture*
per cm&t
83
84
88
84
87
90
87
89
87
89
613
BLOCK
for Growing
- -
Averages............
J.
per
cent
67
71
73
68
67
65
67
66
68
69
67
67
90.6
67.9
mixture
Period No.
Bic$&al
91
89
90
93
90
91
90
91
90
89
91
92
Oat-corn-rye
of Uncooked
TW.5
--
--
digestibility
ger
-_
3
3
3
3
3
3
1
1
1
1
1
1
-_
cent
per cent
90
92
91
92
93
93
91
93
92
94
92
93
63
63
62
63
62
64
64
64
67
71
63
63
92.2
64.1
55
57
59
61
63
56
58
60
62
64
Value
Flour
R.
614
AMINO
ACIDS
IN
PROTEINS
TABLE
Replacement
Value oj Nitrogen
of Processed
Oat-Corn-Rye
Mixture*
on That of
Un,processed
for Adult
Male
Rats, Comparing
Each Rat with Its
11lixture
Pair Mate in Same Experimental
Period
-r
Source
Rat Wo.
Nitrogen
intake per
day
of protein
Nitrogen
balance
per day
.
21
22
23
24
25
26
27
28
29
30
21
22
23
24
25
26
27
2s
29
30
Processed
Unprocessed
Processed
Unprocessed
Processed
Unprocessed
Processed
Unprocessed
Processed
Unprocessed
Unprocessed
Processed
Unprocessed
Processed
Unprocessed
Processed
Unprocessed
Processed
I-nprocessed
Processed
mix
mix
mix
mix
mix
mix
mix
mix
mix
mix
mix
mix
mix
mix
mix
mix
mix
mix
mix
mix
mg.
w.
119
120
119
120
119
120
119
120
117
i
12s
84
84
84
84
84
84
84
84
90
91
+2.31
+15.58
+3.86
+22.58
-4.66
+25.64
+1.63
+15.06
+2.44
-2.91
+9.57
-9.24
+6.59
-8.31
-2.00
-s.75
+1.82
-8.16
+1.66
-11.98
Average.................,.,..,.........,...........................
* Puffed
oat cereal
No.
/
.j-
Difference
nitrogen
balance
mc.
in
:eplacement
ValW
fier cent
13.27
89
18.72
84
30.30
75
13.43
89
-5.35
18.81
104
78
14.90
82
6.75
92
9.98
88
13.64
85
86.6
1.
somewhat more digestible proteins than rolled oats, but with a somewhat
inferior
biological
vahe
(Table
TIII).
Perior
No.
H.
H.
MITCHELL
AND
R.
J.
BLOCK
615
cereal mixture,
for which data are reported
in Table V,
rats) with a 1: 1 milk-cream
mixture
in the proportion
of
of milk-cream,
exhibited
a protein
digestibility
of 93 per
of 85. These
values
apply,
of course,
to the mixed
616
AMINO
ACIDS
IN
TABLE
Amino
Acid
PROTEINS
IX
Content
Oat-Corn-Rye
Amiio
Unprocessed
_-
_per CWCC
acid
per Gent
5.4
2.0
2.0
4.1
5.5
1.1
1.7
2.4
3.9
8.7
5.4
6.0
5.0
2.1
2.2
4.0
6.0
1.1
1.5
2.5
3.5
8.8
5.4
5.8
5.8
1.9
1.9
4.1
5.4
1.1
1.4
2.1
3.2
8.9
4.9
5.5
Amino
Acid
Methods
Kossel-Block isolation
I
I
I
Millon-Lugg
calorimetric
Kapeller-Adler
Millon-Lugg
Fleming-Vassel
McCarthy-Sullivan
colorimetric
Block-Nicolet
oxidation
Microbiological
Phenylalanine. .
Threonine. .....
Leucine ........
Isoleucine......
Valine ..........
Type
of hydrolysis
--
Tryptophane ...
Cystine. .......
....
Methionine.
_-
per cent
Method
Arginine .......
Histidine. ......
Lysine.........
Tyrosine .......
oats
per cent
TABLE
Pelleted
and
exploded
No. of
replicate
leterminations
8 N HzSOd
8
8
5 NaOH
5
I
5
Formic acid-HCI
18% HCl
4
4
4
8
12
8
8
6
18
6
20
20
20
3N
3
3
proteins
5.0
1.9
2.1
4.3
5.6
1.1
1.6
2.4
3.6
8.8
5.6
6.2
Rolled
Pelleted
Amino
Mixture*
acid
Arginine ..............
Histidine. .............
Lysine ................
Tyrosine ..............
Phenylalanine
.........
Tryptophane ..........
Cystine. ..............
Methionine ............
Threonine. ............
Leucine ...............
Isoleucine .............
Valine .................
to
H.
H.
MITCHELL
AND
R.
J.
BLOCK
617
SUMMARY
618
AMINO
ACIDS
IN
PROTElNS
BIBLIOGRAPHY
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ture, such as that of whole egg, that is almost completely digestible by the
rat and utilizable in adolescent metabolism.
This has been done for a series
of twenty-eight
proteins and protein mixtures for which satisfactory
analyses have been secured for a.11of t.he essential amino acids.
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6. In particular, the nutritive
value of cereal proteins may be greatly
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food prot,ein is suggested.
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AND
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619
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