ENDOGENOUS PROTEIN-PHOSPHORYLATION IN PURIFIED PLANT-MITOCHONDRIA

被引：25

作者：

SOMMARIN, M

PETIT, PX

MOLLER, IM

机构：

[1] UNIV PARIS 06,BIOL VEGETALE LAB 4,CNRS,UNITE 1180,F-75230 PARIS 05,FRANCE

[2] UNIV LUND,DEPT PLANT PHYSIOL,S-22007 LUND 7,SWEDEN

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1990年 / 1052卷 / 01期

关键词：

(Plant mitochondria); Protein phosphorylation;

D O I：

10.1016/0167-4889(90)90076-P

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Purified mitochondria from potato (Solanum tuberosum L. cv Bintje) tubers were incubated with [γ-32P]ATP. Total 32P incorporation into proteins saturated after about 2 min and showed a Km (ATP) of 0.2 mM and a broad pH optimum of 6.5-8. About 30 polypetides were labelled as shown by SDS-PAGE and autoradiography. The major labelled polypeptides were at 11, 14, 16 22-23, 40, 42 (the α-subunit of the pyruvate dehydrogenase complex), 45-46, 60, 62, 69, 84-86 and 97 kDa. By the use of atractylate, EGTA and trypsin the major phosphoproteins of 40 and 42 kDa and possibly some minor phosphoproteins in the range 26-33 kDa were localized to the matrix or the inner surface of the inner membrane. All other labelled polypeptides as well as (at least) two kinases (one Ca2+-dependent, the other Ca2+-independent) are outside the inner membrane. © 1990.

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页码：195 / 203

页数：9

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