Analysis of Rat Caseins by High Performance Liquid Chromatography

Hobbs, Andrew A.; Grego, Boris; Smith, May; Hearn, Milton Thomas William

doi:10.1080/01483918108059962

Cited by 10 publications

(1 citation statement)

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“…Reversed-phase HPLC (RP HPLC) has been used to separate milk proteins and their fragments (Diosady and Bergen, 1980; Hobbs et al, 1981;Pearce, 1983;Carles andRibadeau Dumas, 1984,1985) and to determine the kinetic parameters relative to the action of chymosin on the most sensitive bonds of asl-, /3-, and /c-caseins (Carles andRibadeau Dumas, 1984, 1985). In our work RP HPLC analysis of gastric effluents has given quantitative information about the overall process of gastric digestion of caseins, which includes hydrolysis by gastric proteinases, casein retention in the form of coagulum (in the presence of calcium) or of precipitate (by acidification), and gastric emptying.…”

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confidence: 99%

Characterization and kinetics of evacuation of peptides resulting from casein hydrolysis in the stomach of the calf

Yvon¹,

Pélissier²

1987

J. Agric. Food Chem.

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A quantitative method for HPLC analysis of the peptides was developed in order to quantify and to compare the peptides leaving the abomasum of preruminant calves fed three different diets: skim milk, aqueous casein solution, casein solution in a mineral medium simulating ultrafiltered milk permeate. It was found that during the first phase of the digestion (0-90 min) the main peptides released from the two casein diets were fragment 106-169 of /c-casein (casein macropeptide, CMP), fragments 1-23 and 165-199 of a8l-casein, and fragment 193-209 of /3-casein. During the same period, slightly more CMP was released after ingestion of skim milk, while the amounts of the other fragments were respectively 10, 2, and 2 times lower than those obtained with casein diets. Thus, CMP was almost the only peptide to be released during the first hour. After that, casein was degraded into small peptides with the three diets, but the amounts released with skim milk were slower than with casein solutions. It was concluded that coagulation contributed to slow down casein degradation and also to retain some peptides. It was supposed that the stomach's role is not only to regulate the release of milk protein but also to select peptides that enter the gut. Taking into consideration the kinetics of liberation of some particular casein peptides, their supposed physiological activities such as regulation in gastric and pancreatic secretions, morphine-like activity, and role in calcium transport were discussed.

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confidence: 99%