Insoluble pronase

Efficacy and pharmacological mechanism of pronase-enhanced

Chemical modification of aminopeptidase isolated from Pronase.

Chemical modification of aminopeptidase from pronase has revealed two important histidines in enzyme catalysis. In the absence of metal ions, modification of the readily-modified histidine (pKa 6.9 +/- 0.5) results in a drastic loss of activity, indicating that this residue is indispensible for enzyme activity. In the presence of CaCl2, the modified enzyme still retains approx. 60% of the activ...

Analysis of insoluble proteins.

The analysis of insoluble proteins represents a major technical challenge for the field of proteomics. For example, membrane proteins are often insoluble in common solvents and represent 20-30% of the proteins encoded by the human genome. Chemical analysis on an individual basis is often required and is laborious and time consuming. This review presents an overview of methods for purification o...

Pronase destroys the lipopolysaccharide receptor CD14 on Kupffer cells.

CD14 is a lipopolysaccharide (LPS) receptor distributed largely in macrophages, monocytes, and neutrophils; however, the role of CD14 in activation of Kupffer cells by LPS remains controversial. The purpose of this study was to determine if different methods used to isolate Kupffer cells affect CD14. Kupffer cells were isolated by collagenase (0.025%) or collagenase-Pronase (0.02%) perfusion an...

Characterization of membrane-associated Clostridium perfringens enterotoxin following pronase treatment.

After binding, Clostridium perfringens enterotoxin (CPE) initially localizes in a small (approximately 90-kDa) complex in plasma membranes. This event is followed by formation of a second membrane complex, referred to as large (160-kDa) complex. Contrary to a previous hypothesis proposing that CPE inserts into intestinal brush border membranes (BBMs) when this toxin is localized in the small co...