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Purification and enzymatic characterization of a novel metalloprotease from Lachesis muta rhombeata...

Purification and enzymatic characterization of a novel metalloprotease from Lachesis muta rhombeata...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_c438c263bc0847a789ee88fdad8f5a5a

Purification and enzymatic characterization of a novel metalloprotease from Lachesis muta rhombeata snake venom

About this item

Full title

Purification and enzymatic characterization of a novel metalloprotease from Lachesis muta rhombeata snake venom

Publisher

Brazil: Center for the Study of Venoms and Venomous Animals

Journal title

The journal of venomous animals and toxins including tropical diseases, 2018, Vol.24 (1), p.32-32, Article 32

Language

English

Formats

Publication information

Publisher

Brazil: Center for the Study of Venoms and Venomous Animals

More information

Scope and Contents

Contents

(Lmr) is the largest venomous snake in Latin America and its venom contains mainly enzymatic components, such as serine and metalloproteases, L-amino acid oxidase and phospholipases A
. Metalloproteases comprise a large group of zinc-dependent proteases that cleave basement membrane components such as fibronectin, laminin and collagen type IV. T...

Alternative Titles

Full title

Purification and enzymatic characterization of a novel metalloprotease from Lachesis muta rhombeata snake venom

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_c438c263bc0847a789ee88fdad8f5a5a

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_c438c263bc0847a789ee88fdad8f5a5a

Other Identifiers

ISSN

1678-9199

E-ISSN

1678-9199

DOI

10.1186/s40409-018-0171-x

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