Literature DB >> 3977909

Analysis of neuraminidase isozyme phenotypes in mammalian tissues: an electrophoretic approach.

P B Samollow, J L VandeBerg, H W Kunz, T J Gill.   

Abstract

A simple cellulose acetate electrophoretic method for visualizing mammalian neuraminidase isozymes has been developed. Application of the method with rat and mouse liver extracts reveals the presence of two distinct isozymes in each species. Each isozyme exhibits tremendous variation in activity between inbred strains. The two isozymes vary independently of one another suggesting that their activities are controlled by different genes. The neuraminidase phenotypes detected in these inbred strains via electrophoresis are consistent with published accounts of neuraminidase phenotypes determined fluorometrically in whole liver homogenates, but also indicate the presence of a second isozyme not perceived by this other procedure.

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Year:  1985        PMID: 3977909     DOI: 10.1016/0006-291x(85)90310-9

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


  3 in total

1.  Mobilization of sialidase from intracellular stores to the surface of human neutrophils and its role in stimulated adhesion responses of these cells.

Authors:  A S Cross; D G Wright
Journal:  J Clin Invest       Date:  1991-12       Impact factor: 14.808

2.  Mapping the Neu-1 locus to the major histocompatibility complex (RT1) in the rat.

Authors:  P B Samollow; A L Ford; H W Kunz; T J Gill
Journal:  Immunogenetics       Date:  1987       Impact factor: 2.846

3.  Cellular localization and substrate specificity of isoelectric forms of human liver neuraminidase activity.

Authors:  J Spaltro; J A Alhadeff
Journal:  Biochem J       Date:  1987-01-01       Impact factor: 3.857

  3 in total

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