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Kinetics of a micelle specific palmitoyltransferase isoenzyme of rabbit mammary gland
Author(s) -
Caffrey Martin,
Kinsella John E.
Publication year - 1977
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02533381
Subject(s) - micelle , isozyme , chemistry , biochemistry , saturation vapor curve , kinetics , clinical chemistry , substrate (aquarium) , enolase , chromatography , enzyme , biology , organic chemistry , immunohistochemistry , immunology , physics , quantum mechanics , aqueous solution , ecology
Abstract Palmityl‐CoA: monopalmityl‐ sn ‐glycerol 3‐phosphate palmitoyltransferase [EC 2.3.1.‐] in rabbit mammary gland microsomes is composed of two isoenzymic species. The α form (LPAT‐α) is active with monomeric substrates and inhibited by micelles while the β form (LPAT‐β) is active only with micelles. By combining the effects of time, temperature, and Tween 80 which selectively inhibited LPAT‐α, the substrate saturation curve for the LPAT‐β isoenzyme has been successfully determined. Both theoretical and experimental curves are in good agreement.