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Title Transcription
ダイチョウキン K 12 ト ソノ L FORM NC7 ノ マク ケツゴウセイ ATPASE ノ セイシツ
Title Alternative (English)
Properties of membrane bound ATPase in Escherichia coli K12 and its L-form NC7
File
language
eng
Author
Nakano, Shigeru
Onoda, Tetsuo
Description
Membrane bound ATPase of L-form NC7 exhibited a pH optimum of ca. 9.0, and hydrolyzed selectively ATP with the Km value of 0.55 mM. ADP inhibited competitively the hydrolysis of ATP with the Ki value of 0.22 mM. Ca^<2+> and Mg^<2+> as divalent cation were required for the activation of this enzyme, and of these cations optimal molar ratio to ATP were 4 : 5 in calcium at pH 8.5 and about 2 : 5 in magnesium. In the presence of calcium, the enzyme was inhibited by increased concentration of monovalent cations, although in the presence of magnesium, the enzyme was relatively insensitive to their ions. Azide, PCMB and DCCD strongly inhibited the enzyme activity. The enzyme was labile under the temperature below 0-4℃, but addition of 20% methanol to the storage buffer prevented it from their inactivation. The enzyme was stable when it was preincubated below 60℃ for 5 mim. Membrane bound ATPase of L-form NC7 was essentially similar to that of wild type.
Journal Title
Memoirs of the Faculty of Science, Shimane University
Volume
22
Start Page
113
End Page
121
ISSN
03879925
Published Date
1988-12-25
NCID
AN00108106
Publisher
島根大学理学部
Publisher Aalternative
The Faculty of Science, Shimane University
NII Type
Departmental Bulletin Paper
OAI-PMH Set
Faculty of Science and Engineering
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