Purification and characterization of the soluble form of mitochondrial adenosine triphosphatase from sweet potato.

Abstract:

:The soluble form of mitochondrial adenosine triphosphatase was purified in an electrophoretically and immunologically pure form from sweet potato root tissue. The enzyme consisted of six kinds of subunits with different molecular weights (52,500, 51,500, 35,500, 26,000, 23,000, and 12,000), and its molecular weight was about 370,000. Adenosine triphosphatase associated with the submitochondrial particles was oligomycin-sensitive and heat-labile, whereas the soluble form of the enzyme was oligomycin-insensitive and cold-labile. The enzyme in either the membrane-bound or the soluble form showed negative cooperativity. Both experiments with polyacrylamide gel electrophoresis and immunological methods suggest that some of the subunits, probably those with molecular weights of 52,500 and 51,500, are dissociated from the enzyme protein during storage of the enzyme preparations.

journal_name

Arch Biochem Biophys

authors

Iwasaki Y,Asahi T

doi

10.1016/0003-9861(83)90359-4

subject

Has Abstract

pub_date

1983-11-01 00:00:00

pages

164-73

issue

1

eissn

0003-9861

issn

1096-0384

pii

0003-9861(83)90359-4

journal_volume

227

pub_type

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