Home
Resources
Publications
Isolation of Two Forms of Carboxylester Lipase (Cholesterol Esterase) From Porcine Pancreas

Isolation of Two Forms of Carboxylester Lipase (Cholesterol Esterase) From Porcine Pancreas

E A Rudd, N K Mizuno, H L Brockman

Biochim Biophys Acta. 1987 Apr 3;918(2):106-14.

PMID: 3828371

Abstract:

Carboxylester lipase (cholesterol esterase, EC 3.1.1.13) has been purified to homogeneity from porcine pancreas. The enzyme is isolated in two molecular mass forms, a monomer of 74 kDa and a dimer of 167 kDa. The dimer consists of two catalytically-active subunits which have molecular masses approximately 9 kDa greater than the monomers. The difference in size was not attributable to carbohydrate or lipid content. The catalytic properties of the two forms are comparable on a weight basis, the amino acid compositions are quite similar, and the N-terminal sequences are nearly identical for 24 residues. These similarities suggest a possible precursor-product relationship between the two carboxylester lipase forms.

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: