The amino acid sequence of goat alpha-lactalbumin |
| |
Authors: | R T MacGillivray K Brew K Barnes |
| |
Institution: | Department of Biochemistry, University of Miami School of Medicine, Miami, Florida 33101 U.S.A. |
| |
Abstract: | The amino acid sequence of goat α-lactalbumin has been established from the structures of peptides isolated from trypsin and thermolysin digests of the reduced aminoethylated protein and from a chymotrypsin digest of the reduced carboxamidomethylated protein. The amino-terminal sequence was confirmed by automatic sequencer analysis. Of the previously sequenced species variants of α-lactalbumin, the bovine protein is most similar to the goat, differing in only 12 amino acid substitutions. One difference between these proteins corresponds to a substitution found in the bovine A genetic variant (Arg10 → Gln). The relevance of the structure to the evolutionary relationships in the α-lactalbumin-lysozyme family of proteins is discussed. |
| |
Keywords: | |
本文献已被 ScienceDirect 等数据库收录! |