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Article

Effect of genetic variation on the tryptic hydrolysis of bovine beta-lactoglobulin A, B, and C.

Journal of dairy science - 1 Dec 2004

Creamer L K, Nilsson H C, Paulsson M A, Coker C J, Hill J P, Jiménez-Flores R

Abstract excerpt

The structure, stability, and hydrolysis characteristics of beta-lactoglobulin (LG) A are different from those of either beta-LG B or beta-LG C. Purified samples of these proteins were hydrolyzed with trypsin and the rates of loss of native monomeric beta-LG structure were measured using sodium dodecyl sulfate PAGE. At the same time, the appearance of many individual peptides were identified and followed in time...

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Share to Chromatography, High Pressure Liquid
Share to Electrophoresis, Polyacrylamide Gel

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Gas Chromatography-Mass Spectrometry

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Source

Identifiers

PMID: 15545362
DOI: 10.3168/jds.S0022-0302(04)73543-2

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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