scholarly journals Isolation, composition and ordering of cyanogen bromide peptides in human casein

1978 ◽  
Vol 169 (2) ◽  
pp. 337-342 ◽  
Author(s):  
M L Groves ◽  
R Greenberg

The major component of the casein fraction of human milk was cleaved by cyanogen bromide, and the composition of the resulting peptides was determined. Casein was also subjected to limited digestion by trypsin, and the amino acid composition of the isolated peptides was established. With this information the peptides were ordered as they occur in the purified protein.

2009 ◽  
Vol 23 (S1) ◽  
Author(s):  
Ping Feng ◽  
Ming Gao ◽  
Timothy Holley ◽  
TianHui Zhou ◽  
Anita Burgher ◽  
...  

InterConf ◽  
2021 ◽  
pp. 363-369
Author(s):  
Nadira Turganbaeva ◽  
Dinara Isakova

The objective of this paper was to study the amino acid composition of donkey milk inhabiting the Kegety gorge of the Chui region. As well as human milk, donkey and mare’s milk is albumin; the amount of casein is 35-45%, while cow’s milk is casein milk with casein content over 75%. The peculiarity of albumin milk is a higher biological and nutritional value, due to better amino acid balance, high sugar content and the ability to form small, delicate flakes when souring. In terms of its properties, albumin milk is closest to human milk and is the best substitute for it. The obtained results showed that the quantitative content of 7 essential amino acids out of 8, such as lysine, phenylalanine, leucine, isoleucine, methionine, valine, threonine is relatively high compared to other amino acids. Despite the absence of tryptophan in donkey milk, the percentage of 8 essential amino acids in donkey milk protein exceeds that in mare and cow’s milk.


PEDIATRICS ◽  
1954 ◽  
Vol 14 (3) ◽  
pp. 284-284

Volume 12, Oct. 1953, No. 4, page 354, "Total Amino Acid Composition in Mature Human Milk" by Mung W. Cheung, M.D., Edward L. Pratt, M.D., and Dorothy I. Fowler, B.Sc. The value for methionine in our original paper does not include its oxidized product, methionine sulfoxide. In our chromatograms, this compound appears as a skewed peak, suggesting that it contains more than a single substance. However, if this possibility is disregarded and the methionine sulfoxide calculated as methionine, Pool A would have a value for methionine of 19.4 instead of 15.4 mg./100 cc. milk; and Pool B a value of 18.1 instead of 14.3 mg./100 cc. milk. The average total value for methionine of 18.8 mg./100 cc. milk is thus closer to those reported by P. Soupart, Stanford Moore, and E. J. Bigwood, J. Biol. Chem. 206:699, 1954, for human milk analyzed by the ion exchange technic which we employed. [SEE TABLE I IN SOURCE PDF].


1998 ◽  
Vol 80 (1) ◽  
pp. 25-34 ◽  
Author(s):  
Alison J. Darragh ◽  
Paul J. Moughan

Human milk was collected from women in their 10th–14th weeks of lactation, and was analysed for amino acids. Corrections were made for losses of amino acids which were presumed to occur during acid hydrolysis, using a non-linear mathematical model that describes the simultaneous processes of amino acid yield and decay. The mean amino acid composition of the human milk was found to be similar to previously reported estimates, although the cysteine content of the human milk in the present study was 20% higher than the average literature estimate. True (corrected for endogenous amino acid excretions) ileal amino acid digestibility of human milk was determined using the 3-week-old piglet as a model animal for the human infant. The piglets were given either human milk (n 6) or a protein-free diet (n 6) for a 6 d experimental period. Cr2O3 was added as an indigestible marker, to both the human milk and protein-free diet. At the end of the experimental period the piglets were anaesthetized and samples of digesta removed from the terminal ileum of each piglet. After sampling the piglets were killed. Endogenous ileal excretions of amino acids were determined in piglets fed on the protein-free diet. The true digestibilities of total N and amino acid N were 88% and 95% respectively. The true ileal digestibility of the non-amino acid N fraction in human milk, when calculated by difference was only 50%. The true digestibility of the amino acids in human milk ranged from 81–101% with threonine (86%) being the least digestible essential amino acid. When the true ileal digestibility values were used to correct the amino acid composition of human milk, the pattern of digestible amino acids in human milk was different compared with the currently recommended pattern of amino acid requirements for the infant.


2016 ◽  
Vol 60 (1) ◽  
pp. 31042 ◽  
Author(s):  
Ping Feng ◽  
Ming Gao ◽  
Anita Burgher ◽  
Tian Hui Zhou ◽  
Kathryn Pramuk

1986 ◽  
Vol 64 (12) ◽  
pp. 3043-3046
Author(s):  
J. H. Tremaine ◽  
W. P. Ronald

The proteins of turnip rosette virus (TRosV) a sobemovirus, and the Prunus strain of tomato bushy stunt virus (TBSV-P) were cleaved with cyanogen bromide, and highly basic peptides were isolated by ion-exchange chromatography. The amino acid composition and sodium dodecyl sulphate – polyacrylamide gel electrophoresis indicated the basic peptide from TRosV had 40 amino acid residues, including 11 basic residues. This peptide had a composition similar to basic peptides isolated from the sobemoviruses, sowbane mosaic virus, and two strains of southern bean mosaic virus. The amino acid composition and size of the basic peptide from TBSV-P were similar to those found for the amino terminal sequence of the type strain of TBSV.


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