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Titolo:
BINDING OF LIPOPROTEIN-LIPASE TO HEPARIN - IDENTIFICATION OF 5 CRITICAL RESIDUES IN 2 DISTINCT SEGMENTS OF THE AMINO-TERMINAL DOMAIN
Autore:
HATA A; RIDINGER DN; SUTHERLAND S; EMI M; ZHANG SH; MYERS RL; REN KS; CHENG T; INOUE I; WILSON DE; IVERIUS PH; LALOUEL JM;
Indirizzi:
UNIV UTAH,HLTH SCI CTR,ECCLES INST HUMAN GENET,HOWARD HUGHES MED INSTSALT LAKE CITY UT 84132 UNIV UTAH,HLTH SCI CTR,HOWARD HUGHES MED INST SALT LAKE CITY UT 84132 UNIV UTAH,HLTH SCI CTR,VET AFFAIRS MED CTR SALT LAKE CITY UT 84132 UNIV UTAH,HLTH SCI CTR,DEPT HUMAN GENET SALT LAKE CITY UT 84132 UNIV UTAH,HLTH SCI CTR,DEPT INTERNAL MED,DIV SOCIAL MED SALT LAKE CITY UT 84132
Titolo Testata:
The Journal of biological chemistry
fascicolo: 12, volume: 268, anno: 1993,
pagine: 8447 - 8457
SICI:
0021-9258(1993)268:12<8447:BOLTH->2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
HEPATIC TRIGLYCERIDE LIPASE; HUMAN POSTHEPARIN PLASMA; RADIATION INACTIVATION; MOLECULAR-PROPERTIES; ADIPOSE-TISSUE; BOVINE-MILK; SECONDARY-STRUCTURE; KINETIC-PROPERTIES; PANCREATIC LIPASE; CDNA SEQUENCE;
Tipo documento:
Article
Natura:
Periodico
Citazioni:
64
Recensione:
Indirizzi per estratti:
Citazione:
A. Hata et al., "BINDING OF LIPOPROTEIN-LIPASE TO HEPARIN - IDENTIFICATION OF 5 CRITICAL RESIDUES IN 2 DISTINCT SEGMENTS OF THE AMINO-TERMINAL DOMAIN", The Journal of biological chemistry, 268(12), 1993, pp. 8447-8457

Abstract

Binding to heparan sulfate governs many aspects of the physiological action and regulation of the lipolytic enzyme, lipoprotein lipase (LPL). In an attempt to identify the structural determinants which mediatethis interaction, basic residues in three segments of the primary sequence of human LPL (residues 147-151, 279-282, and 292-304) were replaced with alanine, either singly or in various combinations, and variant proteins were subjected to affinity chromatography on heparin-Superose. Five basic residues in two distinct segments of the primary sequence were critical determinants of the high affinity for heparin manifested by the active enzyme (R279, K280, R282, K296, R297). By contrast, no such evidence could be detected for basic residues in the first cluster (K147, K148) or for other basic residues in the third cluster (K292, R294, K304), while the evidence for K300 was unresolved. The conformation of this heparin-binding domain can be inferred by reference tothe three-dimensional structure of the homologous enzyme, pancreatic lipase (Winkler, F. K., D'Arcy, A., and Hunziker, W. (1990) Nature 343, 771-774). Affinity of the active enzyme for heparin could not be reduced below a threshold, suggesting that other heparin-binding determinants exist elsewhere in the molecule, as supported by recently published evidence (Davis, R. C., Wong, H., Nikazy, J., Wang, K., Han, Q., and Schotz, M. C. (1992) J. Biol. Chem. 267, 21499-21504).

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Documento generato il 20/01/21 alle ore 15:53:00