Literature DB >> 3971980

The primary structure of alpha-lactalbumin from camel milk.

O U Beg, H von Bahr-Lindström, Z H Zaidi, H Jörnvall.   

Abstract

The primary structure of camel alpha-lactalbumin was determined by analysis of the intact protein, and of CNBr fragments and enzymatic peptides from the carboxymethylated protein chain. Results show that camel alpha-lactalbumin has 123 residues and a molecular mass of 14.6 kDa. The amino acid sequence is strictly homologous to alpha-lactalbumins characterized, but also exhibits extensive differences: 39 residues differ in relation to the bovine protein and only 35 residues are conserved among hitherto known alpha-lactalbumins with characterized structures. All residues ascribed critical structural or functional roles are strictly invariant in the camel protein.

Entities:  

Mesh:

Substances:

Year:  1985        PMID: 3971980     DOI: 10.1111/j.1432-1033.1985.tb08741.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  3 in total

1.  Ancient origin of lactalbumin from lysozyme: analysis of DNA and amino acid sequences.

Authors:  E M Prager; A C Wilson
Journal:  J Mol Evol       Date:  1988       Impact factor: 2.395

2.  The complete primary structure of late lactation protein from quokka (Setonix brachyurus).

Authors:  O U Beg; D C Shaw
Journal:  J Protein Chem       Date:  1994-08

3.  Comparison of the Allergenicity and Immunogenicity of Camel and Cow's Milk-A Study in Brown Norway Rats.

Authors:  Natalia Zofia Maryniak; Egon Bech Hansen; Anne-Sofie Ravn Ballegaard; Ana Isabel Sancho; Katrine Lindholm Bøgh
Journal:  Nutrients       Date:  2018-12-04       Impact factor: 5.717

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.