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PMID: 6892817 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Use of immobilized lactoperoxidase to label L cell proteins involved in adhesion to polystyrene.

The Journal of cell biology ·Vol. 85 ·No. 2 ·1980-05-00 ·Pages 402-13

Chin NW, Lanks KW

Abstract

Proteins involved in the attachment of murine L cells to polystyrene have been identified by a technique designed to iodinate only those macromolecules coming into closet apposition to the substratum. Whereas soluble lactoperoxidase (LPO) catalyzes the radioiodination of a broad spectrum of polypeptides, the same enzyme immobilized on polystyrene tissue culture flasks discriminately labels 55,000 and 42,000 mol wt polypeptides that adhere tightly to the substratum after the cells are removed. One-dimensional peptide mapping following limited proteolysis showed that the labeled 55,000 mol wt polypeptide is similar to a component of comparable molecular weight present in the detergent-extracted cytoskeleton. The functional association of two cytoskeletal structures, presumably 10-nm filaments and actin, is discussed, and alternative explanations for their susceptibility to iodination by immobilized LPO are presented.

MeSH Terms
Actins/physiology Animals Cell Adhesion Cytoskeleton/physiology Enzymes, Immobilized L Cells Lactoperoxidase Membrane Proteins/analysis,physiology Mice Molecular Weight Peptides/analysis Polystyrenes
Chemicals
Actins Enzymes, Immobilized Membrane Proteins Peptides Polystyrenes Lactoperoxidase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Chin N W
Lanks K W
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46 references, click to expand
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
DOI
10.1083/jcb.85.2.402
Published
1980-05-00
Pages
402-13
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2110604
Subset
IM
External Links
PubMed source DOI: 10.1083/jcb.85.2.402 PMC Full Text View journal details
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