Two forms of restriction enzyme HindIII.

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Two forms of restriction enzyme HindIII. Abstract Text:

Y Takasaki,

Restriction endonuclease HindIII was purified from Haemophilus influenzae Rd. Two active fractions, P1 and P2, were obtained in phosphocellulose chromatography. HindIII could be purified completely from the first fraction, P1, by subsequent DEAE-cellulose chromatography. The second fraction, P2, showed HindIII activity higher than that of P1, though it was still contaminated with some minor proteins. The HindIII in P2 fraction showed differences in stability, binding to substrate DNA, electrophoretic mobility, etc., from the HindIII in P1 fraction. It is likely that there are two forms of HindIII in the bacterial cell. The endonuclease HindIII in P2 fraction was finally purified by DNA-cellulose chromatography, though considerable loss of enzymatic activity resulted. Upon infection of the cells with phage T4, the P2 fraction in phosphocellulose chromatography almost disappeared. The presence of two forms of HindIII may be related to bacterial defense against viral infection.

Two forms of restriction enzyme HindIII. Publishing Authors By Initials

Y Takasaki,

For similar enzymes and coenzymes: enzymes: isoenzymes research abstracts see: enzymes and coenzymes: enzymes: isoenzymes research

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Two forms of restriction enzyme HindIII. Journal Published:

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

Journal: Journal of biochemistry

VOLUME: 116

Page Numbers: 1281-6

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Dec

YEAR: 1994

Two forms of restriction enzyme HindIII. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Two forms of restriction enzyme HindIII. Keywords Mesh Terms:

KEYWORDS: Isoenzymes

MESH TERMS: metabolism

Chemical & Substance for Abstract: Two forms of restriction enzyme HindIII. Information

Substance Name: Deoxyribonuclease HindIII

Registry Number: EC 3.1.21.-

Grant and Affiliation Information for Two forms of restriction enzyme HindIII.

AFFILIATION: Chemistry Laboratory, Saga Medical School.

Country: JAPAN

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MEDLINETA: J Biochem

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