Abstract：
:Rabbit muscle lactate dehydrogenase (LDH) was coupled to Sepharose in such a way that each molecule is expected to be attached via only one subunit. Dissociation of the bound active enzyme by several methods all yielded immobilized subunit derivatives which were inactive. These derivatives were capable of regenerating activity by interacting specifically with subunits in solution formed transiently during renaturation. This ability to peck up soluble subunits is lost fairly rapidly upon storage of the immobilized subunits. Similarly, LDH subunits attached to Sepharose via disulfide bonds were found to be inactive. When these subunits were detached from the matrix by mild reduction with mercaptoethanol, activity was regenerated. The kinetics of this reactivation process suggests that reassociation is required for appearance of activity. All these results can be interpreted as showing that subunit interactions are essential for LDH activity.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Chan WW,Mosbach Kdoi
10.1021/bi00664a013subject
Has Abstractpub_date
1976-09-21 00:00:00pages
4215-22issue
19eissn
0006-2960issn
1520-4995journal_volume
15pub_type
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