Open AccessThe primary structure of α‐lactalbumin from camel milk
Author(s) -
BEG Obaid Ullah,
BAHRLINDSTRÖM Hedvig,
ZAIDI Zafar H.,
JÖRNVALL Hans
Publication year - 1985
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1985.tb08741.x
Subject(s) - lactalbumin , protein primary structure , alpha lactalbumin , chemistry , residue (chemistry) , biochemistry , peptide sequence , amino acid residue , alpha (finance) , protein secondary structure , protein structure , amino acid , camel milk , molecular mass , enzyme , food science , gene , medicine , construct validity , nursing , patient satisfaction
The primary structure of camel α‐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 α‐lactalbumin has 123 residues and a molecular mass of 14.6 kDa. The amino acid sequence is strictly homologous to α‐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 α‐lactalbumins with characterized structures. All residues ascribed critical structural or functional roles are strictly invariant in the camel protein.