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Purification and characterization of a factor stimulating DNA polymerase alpha activity from mouse FM3A cells.

Purification and characterization of a factor stimulating DNA polymerase alpha activity from mouse FM3A cells. Research Abstract Details 

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  • Purification and characterization of a factor stimulating DNA polymerase alpha activity from mouse FM3A cells. Abstract Text:

    k kawasakiK Kawasaki,k nagataK Nagata,t enomotoT Enomoto,f hanaokaF Hanaoka,m yamadaM Yamada,

    A protein factor which stimulates DNA polymerase alpha activity on heat-denatured DNA has been purified from mouse FM3A cells. The final preparation had a specific activity of 43,000 units/mg protein and lacked detectable DNA polymerase, RNA polymerase, DNA-dependent- and independent ATPase, exo- and endodeoxyribonuclease and phosphatase activities. The stimulating factor sedimented at 2.9S in a glycerol gradient. Sodium dodecyl sulfate polyacrylamide gel electrophoresis of the glycerol gradient fraction revealed the presence of a major band of 36,000 daltons, the amount of which corresponded well with the level of stimulating activity. The stimulation by the factor was specific for heat-denatured DNA, and a little or no stimulation was observed with native DNA, ribo- and deoxyribohomopolymers and single stranded circular DNA. Alkaline sucrose gradient sedimentation analysis of the reaction products revealed that newly synthesized DNA was covalently linked to the termini of heat-denatured DNA. The average chain length of the elongated span determined by the digestion with micrococcal nuclease and phosphodiesterase II, did not differ between in the presence and absence of the stimulating factor, suggesting that the stimulation by the factor was due to the increase in the initiation frequency of DNA synthesis from the 3'-hydroxyl terminus of heat-denatured DNA.

    Purification and characterization of a factor stimulating DNA polymerase alpha activity from mouse FM3A cells. Publishing Authors By Initials

    k kawasakiK Kawasaki,k nagataK Nagata,t enomotoT Enomoto,f hanaokaF Hanaoka,m yamadaM Yamada,

    For similar proteins research abstracts see: proteins research

    PUBMED ID PMID:

    MEDLINE DATE:

    Purification and characterization of a factor stimulating DNA polymerase alpha activity from mouse FM3A cells. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Journal of biochemistry

    VOLUME: 95

    Page Numbers: 485-93

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Feb

    YEAR: 1984

    Purification and characterization of a factor stimulating DNA polymerase alpha activity from mouse FM3A cells. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Purification and characterization of a factor stimulating DNA polymerase alpha activity from mouse FM3A cells. Keywords Mesh Terms:

    KEYWORDS: Proteins

    MESH TERMS: isolation & purification

    Chemical & Substance for Abstract: Purification and characterization of a factor stimulating DNA polymerase alpha activity from mouse FM3A cells. Information

    Substance Name: Phosphoric Monoester Hydrolases

    Registry Number: EC 3.1.3.-

    Grant and Affiliation Information for Purification and characterization of a factor stimulating DNA polymerase alpha activity from mouse FM3A cells.

    AFFILIATION:

    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

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    MEDLINETA: J Biochem

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