Lipoprotein lipase: isolation and characterization of a second enzyme species from postheparin plasma. [Rats]
- Univ. of California, San Francisco
A lipoprotein lipase species (mol wt 69 250) has been isolated from rat postheparin plasma, which differs from the low-molecular-weight species previously characterized in its amino acid composition and hexosamine content, and in its lower affinity for triglyceride-rich lipoprotein substrates. However, both enzymes are activated by the same coprotein (C-terminal glutamic acid, apo-C-2) from human very low density lipoprotein and have a similar specificity for lipid esters. Neither purified enzyme is activated by heparin. Both are inhibited by molar sodium chloride. Both enzyme species can be recovered from the same plasma samples. The possible relationship of these proteins to the different functional lipoprotein lipase activities of muscle and adipose tissues is discussed.
- OSTI ID:
- 7008279
- Journal Information:
- Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 16:9; ISSN BICHA
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
59 BASIC BIOLOGICAL SCIENCES
ADIPOSE TISSUE
ALKALI METAL COMPOUNDS
AMINES
ANIMAL TISSUES
ANTICOAGULANTS
BIOLOGICAL MATERIALS
BLOOD
BLOOD PLASMA
BODY
BODY FLUIDS
CARBOHYDRATES
CARBOXYLESTERASES
CHEMICAL ACTIVATION
CHEMICAL COMPOSITION
CHLORIDES
CHLORINE COMPOUNDS
CONNECTIVE TISSUE
DRUGS
ENZYME ACTIVITY
ENZYMES
ESTERASES
HALIDES
HALOGEN COMPOUNDS
HEMATOLOGIC AGENTS
HEPARIN
HYDROLASES
INHIBITION
LIPASE
LIPIDS
LIPOPROTEINS
MATERIALS
MUCOPOLYSACCHARIDES
MUSCLES
ORGANIC COMPOUNDS
ORGANIC SULFUR COMPOUNDS
POLYSACCHARIDES
PROTEINS
SACCHARIDES
SODIUM CHLORIDES
SODIUM COMPOUNDS
SUBSTRATES
TISSUES