Purification and partial characterization of a thiol proteinase from the thermophilic fungus Humicola lanuginosa.
Journal Article (Journal Article)
An extracellular thiol proteinase was produced by the growth of a thermophilic fungus, Humicola lanuginosa, on a medium containing 2% casein, and was purified to virtual homogeneity by affinity chromatography on organomercurial columns. The essential thiol group for activity was confirmed by the inhibition of the enzyme by p-chloromercuribenzoate and mercuric ions. The enzyme, purified 27-fold from the extracellular fluid, exhibited an Mr of 23700 on gel filtration and sedimentation equilibrium. The H. lanuginosa proteinase preferentially cleaves at the C-terminal end of hydrophobic amino acid residues. This proteinase differed from the plant enzyme papain in its interaction with three affinity matrices and its substrate specificity towards synthetic substrates. This enzyme represents a unique example of a thiol proteinase obtained from a fungal source.
Full Text
Duke Authors
Cited Authors
- Shenolikar, S; Stevenson, KJ
Published Date
- July 1, 1982
Published In
Volume / Issue
- 205 / 1
Start / End Page
- 147 - 152
PubMed ID
- 6751320
Pubmed Central ID
- PMC1158457
International Standard Serial Number (ISSN)
- 0264-6021
Digital Object Identifier (DOI)
- 10.1042/bj2050147
Language
- eng
Conference Location
- England