Literature DB >> 3619904

Demonstration of tubulin-glycolytic enzyme interactions using a novel electrophoretic approach.

R Karkhoff-Schweizer, H R Knull.   

Abstract

A gel electrophoretic technique was used to demonstrate an interaction with the soluble enzymes aldolase, glyceraldehydephosphate dehydrogenase, pyruvate kinase and muscle type lactate dehydrogenase to the cytoskeletal protein tubulin. It is suggested that tubulin, like actin, is a key cytoskeletal structure with which soluble proteins may associate.

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Year:  1987        PMID: 3619904     DOI: 10.1016/0006-291x(87)90605-x

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  5 in total

1.  BD SIMULATIONS OF THE IONIC STRENGTH DEPENDENCE OF THE INTERACTIONS BETWEEN TRIOSE PHOSPHATE ISOMERASE AND F-ACTIN.

Authors:  Elizabeth Spanbauer Schmidt; Neville Y Forlemu; Eric N Njabon; Kathryn A Thomasson
Journal:  J Undergrad Chem Res       Date:  2010

2.  Glycolysis in permeabilized L-929 cells.

Authors:  J S Clegg; S A Jackson
Journal:  Biochem J       Date:  1988-10-01       Impact factor: 3.857

3.  Structure of human brain fructose 1,6-(bis)phosphate aldolase: linking isozyme structure with function.

Authors:  Tracy L Arakaki; John A Pezza; Michelle A Cronin; Chris E Hopkins; Danna B Zimmer; Dean R Tolan; Karen N Allen
Journal:  Protein Sci       Date:  2004-11-10       Impact factor: 6.725

4.  Purification and properties of pig liver and muscle enolases.

Authors:  W W Farrar; W C Deal
Journal:  J Protein Chem       Date:  1995-08

5.  One-step purification of assembly-competent tubulin from diverse eukaryotic sources.

Authors:  Per O Widlund; Marija Podolski; Simone Reber; Joshua Alper; Marko Storch; Anthony A Hyman; Jonathon Howard; David N Drechsel
Journal:  Mol Biol Cell       Date:  2012-09-19       Impact factor: 4.138

  5 in total

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