Home
Resources
Publications
Purification and Characterization of Cholesterol Esterase From Porcine Pancreas

Purification and Characterization of Cholesterol Esterase From Porcine Pancreas

W E Momsen, H L Brockman

Biochim Biophys Acta. 1976 Jan 18;486(1):103-13.

PMID: 12831

Abstract:

A protein catalyzing the hydrolysis of cholesterol esters and p-nitrophenyl acetate has been purified 200-fold from porcine pancreas. The enzyme is homogenous as judged by polyacrylamide gel electrophoresis and exhibits a molecular weight of 80 000 as determined by sodium dodecyl sulfate electrophoresis and gel filtration. Activity toward p-nitrophenylacetate exhibits a broad pH optimum and is influenced by a group with a pKa of 5.5--6.0. The enzyme is completely inhibited by diisopropylfluorophosphate at concentrations as low as 10(-5) M, suggesting that it is a serine esterase. Partial inhibition was observed with p-chloromercuribenzoate.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9026000	Cholesterol Esterase from porcine pancreas		9026-00-0	Price

As a specialist in analytical chemical Products, Alfa Chemistry offers consumers a wealth of raw materials and a full range of technologies and services.

QUICK LINKS

HEADQUARTERS

Tel:

Fax:

Email: