Phospholipases as structural and functional probes for circulating lipoproteins

Technical Report · Thu Jan 01 04:00:00 EST 1976

OSTI ID:7351158

Scanu, A M

Studies have shown that enzymatic probes can be applied successfully to the study of the structure and function of circulating lipoproteins. Phospholipase A/sub 2/ permitted highly specific modifications in both low- and high-density lipoproteins, under mild reaction conditions, with no evidence of side reactions. Furthermore, it was possible by the use of this enzyme, to make precise kinetic analyses, and to characterize the substrate particles reisolated following enzymatic digestion. Studies have also shown that the hydrolyzable phospholipids, which are constituents of circulating lipoproteins, are a natural substrate for the enzyme--an observation which suggests that this reaction may have physiological importance in lipoprotein metabolism. The wealth of information derived from the current work ought to encourage precise kinetic analyses of other lipolytic enzymes known to cleave lipid constituents of circulating lipoproteins. The intensive work now being directed at the purification of these enzymes should make possible their use as structural probes to provide an understanding of their physiological role in fat metabolism.

• Research Organization: Chicago Univ., Ill. (USA); Franklin McLean Memorial Research Inst., Chicago, Ill. (USA)
• OSTI ID: 7351158
• Report Number(s): CONF-760635-4
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
BIOCHEMICAL REACTION KINETICS
CLEAVAGE
CRYSTAL STRUCTURE
ENZYMES
ESTERASES
ESTERS
HYDROLASES
KINETICS
LIPASES
LIPIDS
LIPOPROTEINS
METABOLISM
MICROSTRUCTURE
ORGANIC COMPOUNDS
ORGANIC PHOSPHORUS COMPOUNDS
PHOSPHOLIPIDS
PROBES
PROTEINS
PURIFICATION
REACTION KINETICS