A new member of the plasma protease inhibitor gene family

A 2.1-kb cDNA clone representing a new member of the protease inhibitor family was isolated from a human liver cDNA library. The inhibitor, named human Leuserpin 2 (hLS2), comprises 480 amino acids and contains a leucine residue at its putative reactive center. HLS2 is about 25–28% homologous to thr...

Full description

Saved in:
Bibliographic Details
Published in:Nucleic acids research 1986-01, Vol.14 (2), p.1073-1088
Main Author: RAGG, H
Format: Article
Language:English
Subjects:
alpha 1-Antitrypsin - genetics
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Base Sequence
Biological and medical sciences
Blood Proteins
Cloning, Molecular
DNA - analysis
DNA Restriction Enzymes
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Genes
Heparin Cofactor II
Humans
Hydrolases
Liver - metabolism
Nucleic Acid Hybridization
Ovalbumin - genetics
Plasmids
Protease Inhibitors - genetics
Proteins - genetics
Sequence Homology, Nucleic Acid
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:A 2.1-kb cDNA clone representing a new member of the protease inhibitor family was isolated from a human liver cDNA library. The inhibitor, named human Leuserpin 2 (hLS2), comprises 480 amino acids and contains a leucine residue at its putative reactive center. HLS2 is about 25–28% homologous to three huaan members of the plasma protease inhibitor family: antithrombin III, αl-antitrypsin and α-antichymotrypsin. A comparison with published partial amino acid sequences shows that hLS2 is closely related to the thrombin inhibitor heparin cofactor II.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/14.2.1073