Ontology highlight
ABSTRACT:
SUBMITTER: Sasisekharan R
PROVIDER: S-EPMC46361 | biostudies-other | 1993 Apr
REPOSITORIES: biostudies-other
Sasisekharan R R Bulmer M M Moremen K W KW Cooney C L CL Langer R R
Proceedings of the National Academy of Sciences of the United States of America 19930401 8
Heparinases, enzymes that cleave heparin and heparin sulfate, are implicated in physiological and pathological functions ranging from wound healing to tumor metastasis and are useful in deheparinization therapies. We report the cloning of the heparinase I (EC 4.2.2.7) gene from Flavobacterium heparinum using PCR. Two degenerate oligonucleotides, based on the amino acid sequences derived from tryptic peptides of purified heparinase, were used to generate a 600-bp probe by PCR amplification using ...[more]