BROWSE

Related Researcher

Author's Photo

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

ITEM VIEW & DOWNLOAD

INOSITOL PHOSPHOLIPID-SPECIFIC PHOSPHOLIPASE-C - COMPLETE CDNA AND PROTEIN SEQUENCES AND SEQUENCE HOMOLOGY TO TYROSINE KINASE-RELATED ONCOGENE PRODUCTS

Cited 222 times inthomson ciCited 94 times inthomson ci
Title
INOSITOL PHOSPHOLIPID-SPECIFIC PHOSPHOLIPASE-C - COMPLETE CDNA AND PROTEIN SEQUENCES AND SEQUENCE HOMOLOGY TO TYROSINE KINASE-RELATED ONCOGENE PRODUCTS
Author
Suh, Pann-GhillRyu, Sung HoMoon, Kyung HoSuh, Hae WonRhee, Sue Goo
Issue Date
1988-08
Publisher
NATL ACAD SCIENCES
Citation
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.85, no.15, pp.5419 - 5423
Abstract
Antibodies against an inositol phospholipid-specific phospholipase C purified from bovine brain were used to screen rat brain λgt11 expression cDNA libraries. Complete sequences of three cDNA inserts yielded a cumulative sequence of 5106 base pairs. The deduced protein had 1289 amino acids with a calculated molecular weight of 148,431. The determination of an open reading frame was aided by the amino acid sequences of 21 tryptic peptides isolated from bovine brain phospholipase C. Only 9 residues of a total of 140 amino acid residues determined for the bovine enzyme were different from those deduced from the rat cDNA. Two regions of phospholipase C (amino acid residues 555-598 and 668-705) exhibited significant amino acid similarities to the products of various tyrosine kinase-related oncogenes (yes, src, fgr, abl, fps, fes, and tck). The homologous domain was located in the region that is not essential for the protein-tyrosine kinase activity but is likely to be involved in an interaction with cellular components that modulate kinase function. Therefore, this unexpected similarity raises the possibility that the 148-kDa phospholipase C and cytoplasmic tyrosine kinases are modulated by common cellular component(s).
URI
https://scholarworks.unist.ac.kr/handle/201301/16510
URL
http://www.pnas.org/content/85/15/5419
DOI
10.1073/pnas.85.15.5419
ISSN
0027-8424
Appears in Collections:
BIO_Journal Papers
Files in This Item:
There are no files associated with this item.

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

Show full item record

qrcode

  • mendeley

    citeulike

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

MENU