Special Feature

User Panel

My Panel

My Panel

Bookmark Science Articles

Recent News
Bookmark / Share This Science Site

Purification and enzymatic characterization of three endoDNase isoenzymes from Physarum polycephalum.

Purification and enzymatic characterization of three endoDNase isoenzymes from Physarum polycephalum. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

  • Abstract Text of This Paper
  • Journal Published
  • MeSH Keywords of This Abstract
  • Chemicals and Substances Used in this Paper
  • Grants and Granting Agency of this Research
  • Database Accession Numbers Used in this Paper
  • Related Papers
  • Related Research Tags
  • Rate this Research Paper
  • Purification and enzymatic characterization of three endoDNase isoenzymes from Physarum polycephalum. Abstract Text:

    j h waterborgJ H Waterborg,c m kuyperC M Kuyper,

    Three alkaline DNases, A, B, and C, with preference for the digestion of double-stranded DNA (dsDNA) were partially purified from microplasmodia of Physarum polycephalum. They were very similar but differed in their isoelectric points. These were pH 5.8 for DNase A, 7.1 for DNase B, and 9.1 for DNase C. All three enzymes consisted of a single polypeptide chain with a molecular weight of 16,000 to 17,000, which readily formed high molecular weight complexes with low enzyme activity. These complexes could be reversibly dissociated by urea, and DNase activity was quantitatively reactivated. The DNases hydrolyzed the substrate DNA by an endonucleolytic mechanism which gave 5'-phosphorylated products. Divalent cations, MnCl2 or MgCl2, were essential for enzyme activity at the optimum pH of approximately 8.5 and at low ionic strength. The optimal conditions of pH, buffer, divalent cations and ionic strength and the extent of inhibition by salt, phosphate ions or urea differed slightly but significantly between the different isoenzymes.

    Purification and enzymatic characterization of three endoDNase isoenzymes from Physarum polycephalum. Publishing Authors By Initials

    jh waterborgJH Waterborg,cm kuyperCM Kuyper,

    For similar organic chemicals: urea research abstracts see: organic chemicals: urea research

    PUBMED ID PMID:

    MEDLINE DATE:

    Purification and enzymatic characterization of three endoDNase isoenzymes from Physarum polycephalum. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Journal of biochemistry

    VOLUME: 87

    Page Numbers: 651-61

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Feb

    YEAR: 1980

    Purification and enzymatic characterization of three endoDNase isoenzymes from Physarum polycephalum. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Purification and enzymatic characterization of three endoDNase isoenzymes from Physarum polycephalum. Keywords Mesh Terms:

    KEYWORDS: Urea

    MESH TERMS: pharmacology

    Chemical & Substance for Abstract: Purification and enzymatic characterization of three endoDNase isoenzymes from Physarum polycephalum. Information

    Substance Name: Endonucleases

    Registry Number: EC 3.1.-

    Grant and Affiliation Information for Purification and enzymatic characterization of three endoDNase isoenzymes from Physarum polycephalum.

    AFFILIATION:

    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

    AGENCY:

    GRANT:

    ACRONYM:

    MEDLINETA: J Biochem

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

    Purification and enzymatic characterization of three endoDNase isoenzymes from Physarum polycephalum Related Publications

     

    Molecular Station USER Menu

    Welcome to Molecular Station!

    You have to register before you can post on our forums or use our advanced features. Register Now! Its Free and Fast!

    Already registered? Login now below.

    User Name:

    Password:

    Already registered and Forgot your password? Click below to recover it.

    Recover Lost Password

    Join now - it's fast and free!

    Molecular Station is THE largest network of researchers, scientists and science lovers anywhere!

    Research Terms of Usage and Disclaimer
    Home
    Features

    Protocols

    DNA Forum

    Science Forum

    DNA Forum
    Biology Forum

    Science News


    [CaRP] XML error: Invalid document end at line 2

    For more click here:Science News