Amino acid sequence of β‐galactoside‐binding bovine heart lectin

FEBS Letters

Feizi, Ten²  Abbott, William M.²  Childs, Robert A.²  Southan, Christopher¹  Aitken, Alastair¹ 

[1] Cancer Research Campaign Protein Sequencing Facility, Department of Pharmaceutical Chemistry, School of Pharmacy, Brunswick Square, London WC1N 1AX UK;Applied Immunochemistry Research Group, Clinical Research Centre, Northwick Park Hospital, Watford Road, Harrow HA1 3UJ, England

关键词: Lectin;    β-Galactoside binding;    Amino acid sequence;    Sequence homology;    Protein family;   

DOI  :  10.1016/0014-5793(87)80074-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A variety of animal tissues contain β-galactoside-binding lectins with molecular masses in the range 13–17 kDa. There is evidence that these lectins may constitute a new protein family although their function in vivo is not yet clear. In this work the major part of the amino acid sequence of the 13 kDa lectin from bovine heart muscle has been determined. Comparison of this sequence with the cDNA-deduced sequence published for the chick embryo skin lectin showed 58% homology. Comparison of the bovine lectin sequence with partial sequences from two cDNA clones from a human hepatoma library and partial amino acid sequences of human lung lectin showed 70, 40 and 85% homology, respectively. The sequences of these vertebrate lectins are thus clearly related, supporting earlier results of immunological cross-reactivity within this group of proteins. Computer searching of protein sequence databases did not detect significant homologies between the bovine lectin sequence and other known proteins.

【 授权许可】

Unknown