Molecular multiplicity of nuclease TT1 from Thermus thermophilus HB8.

Abstract:

:Purified nuclease TT1 from Thermus thermophilus HB8 has multimolecular weight forms, each of which is composed of three different subunits, alpha (10.8 x 10(4)), beta (7.8 x 10(4)), and gamma (4.1 x 10(4)). The molecular weights of this enzyme were estimated by gel filtration, polyacrylamide gel electrophoresis and equilibrium sedimentation. It was found that most of the enzyme has a molecular weight of about 22 x 10(4) being a monomer having the subunit composition of alpha beta gamma. The remaining part of the enzyme has larger molecular weights and is considered to be size-isomers of alpha beta gamma. The alpha-helical content, 5.5--6.5%, and the beta-structure, about 28%, were estimated from the CD spectrum at 4 degrees C.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Takahashi M,Kobayashi M,Uchida T

doi

10.1093/oxfordjournals.jbchem.a133619

subject

Has Abstract

pub_date

1981-11-01 00:00:00

pages

1521-7

issue

5

eissn

0021-924X

issn

1756-2651

journal_volume

90

pub_type

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