File | |
Title |
大腸菌・L-型菌NC7からのカルシウム結合性タンパク質
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Title |
Study on Calcium-Binding Protein from Escherichia coli L-form NC7
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Title Transcription |
ダイチョウキン Lガタキン NC7 カラノ カルシウム ケツゴウセイ タンパクシツ
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Creator |
Yawata Toshio
Onoda Tetsuo
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Source Title |
島根大学理学部紀要
Memoirs of the Faculty of Science, Shimane University
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Volume | 29 |
Start Page | 37 |
End Page | 43 |
Journal Identifire |
ISSN 03879925
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Descriptions |
A calmodulin-like protein (CaLP) that has been regarded as a Ca2+-dependent modulator protein in Escherichia coli L-form NC7 was purified by fluphenazine-sepharose 4B affinity chromatography. The molecular weight of the CaLP was approx. 18,000 kDa on SDS-Polyacrylamide gel electrophoresis and isoelectric point of 4.5 was confirmed by electric focusing gel (pH 3 to 10). The CaLP were heat stable and exhibited Ca2+-binding property. Further, the CaLP stimulated bovine hart phosphodiesterase activity. These results suggest the presence of Ca2+-regulatory system in prokaryotes.
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Language |
eng
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Resource Type | departmental bulletin paper |
Publisher |
島根大学理学部
The Faculty of Science, Shimane University
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Date of Issued | 1995-12-25 |
Access Rights | open access |
Relation |
[NCID] AN00108106
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