| Literature DB >> 3971980 |
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:
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Year: 1985 PMID: 3971980 DOI: 10.1111/j.1432-1033.1985.tb08741.x
Source DB: PubMed Journal: Eur J Biochem ISSN: 0014-2956