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PMID: 6643497 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Primary structures of MCP-1 and MCP-2, natural peptide antibiotics of rabbit lung macrophages.

The Journal of biological chemistry ·Vol. 258 ·No. 23 ·1983-12-10 ·Pages 14485-9

Selsted ME, Brown DM, DeLange RJ, Lehrer RI

Abstract

The microbicidal peptides, MCP-1 and MCP-2, of rabbit alveolar macrophages were purified by an improved procedure that employed preparative gel electrophoresis and high performance liquid chromatography. The peptides were arginine- and cystine-rich and lacked free sulfhydryl groups and detectable levels of carbohydrate. Complete sequence determinations revealed that MCP-1 differed from MCP-2 only by the substitution of arginine for leucine at residue 13 from the NH2 terminus and that the molecules were each single chain polypeptides of 33 amino acid residues containing three intramolecular disulfide bonds. The complete amino acid sequences of MCP-1 and MCP-2 are: (sequence in text)

MeSH Terms
Amino Acid Sequence Animals Antimicrobial Cationic Peptides Carbohydrates/analysis Lung/analysis Macrophages/analysis Molecular Weight Proteins/analysis Rabbits Sulfhydryl Compounds/analysis
Chemicals
Antimicrobial Cationic Peptides Carbohydrates Proteins Sulfhydryl Compounds
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Selsted M E
Brown D M
DeLange R J
Lehrer R I
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1983-12-10
Pages
14485-9
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Grants
NIAID NIH HHS · AI-16005 · United States
NIAID NIH HHS · AI-16252 · United States
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