BROWSE

Related Researcher

Author

Suh, Pann-Ghill
BioSignal Network Lab (BSN)
Research Interests
  • Signal transduction, cancer, metabolism, phospholipase C

ITEM VIEW & DOWNLOAD

PURIFICATION OF A NOVEL PHOSPHOLIPASE-C ISOZYME FROM BOVINE CEREBELLUM

Cited 27 times inthomson ciCited 21 times inthomson ci
Title
PURIFICATION OF A NOVEL PHOSPHOLIPASE-C ISOZYME FROM BOVINE CEREBELLUM
Author
MIN, DSKIM, DMLEE, YHSEO, JKSuh, Pann-GhillRYU, SH
Keywords
G-PROTEINS; HUMAN-PLATELETS; ALPHA-SUBUNITS; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE; IMMUNOLOGICAL IDENTIFICATION; TYROSINE PHOSPHORYLATION; SIGNAL TRANSDUCTION; BETA-1 ISOZYME; RECEPTOR; BRAIN
Issue Date
199306
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Citation
JOURNAL OF BIOLOGICAL CHEMISTRY, v.268, no.16, pp.12207 - 12212
Abstract
An isozyme of phosphoinositide-specific phospholipase C (PLC) was purified to near homogeneity from bovine cerebellum by a combination of several column chromatography procedures. Approximately 80 mug of pure enzyme were obtained from 4 kg of bovine cerebellum, with a final specific activity of 7.5 mumol/min/mg protein in the presence of 0.1% deoxycholate. The enzyme is specific for phosphatidylinositol and phosphatidylinositol 4,5-bisphosphate but does not hydrolyze phosphatidylcholine. The molecular weight of the enzyme determined by SDS-polyacrylamide gel electrophoresis is approximately 97,000. Polyclonal antibodies to previously characterized PLC isozymes, PLC-beta1,beta2,gamma1,gamma2, and -delta1, did not cross-react with the purified cerebellar enzyme. Moreover, polyclonal antibodies prepared against the cerebellar enzyme did not react with purified PLC-beta1, -beta2, -gamma1, -gamma2, or -delta1. However, the cerebellar enzyme was recognized by two antibodies generated against peptide sequences common to mammalian PLC isozymes. Comparison of partial amino acid sequences of the purified cerebellar enzyme with the deduced amino acid sequence of each known PLC isozyme shows that the cerebellar enzyme is a novel PLC, which could be classified as a PLC-beta-type isozyme. Thus, we have designated this enzyme PLC-beta4.
URI
Go to Link
ISSN
0021-9258
Appears in Collections:
SLS_Journal Papers

find_unist can give you direct access to the published full text of this article. (UNISTARs only)

Show full item record

qr_code

  • mendeley

    citeulike

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

MENU