THE HISTOCHEMICAL PROPERTIES OF THE NEUTRAL PYROPHOSPHATASE ACTIVITY IN LYSOSOMES OF OSTEOCLASTS
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概要
- 論文の詳細を見る
The lysosomal enzyme of osteoclasts which hydrolyze ATP or ADP at the neutral pH range (pH 7.0-7.4) was markedly inhibited by NaF. On the other hand, L-tetramisole or L-cysteine, known to be the inhibitors for the alkaline phosphatase, stabilized or rather increased the enzyme activity. The degree of the activity was moderate to intense when either of them was used solely or with NaF. The thiamine pyrophosphatase activity was also influenced by the above mentioned agents equally as the cases of ATP- or ADP-hydrolysis. The activity of ATP-hydrolysis in lysosomes at pH 8.5 was generally faint, and the inhibitory effect of the same agents seemed to be very weak or non-effective. These histochemical findings led us to conclude that the enzyme dealt with was possibly the neutral pyrophosphatase indicated by the biochemical procedures.
- 日本組織細胞化学会の論文
著者
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Fukushima Osamu
Department Of Anatomy Jikei University School Of Medicine
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Goshi Norihisa
Department Of Anatomy Jikei University School Of Medicine
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Fukushima Osamu
Department Of Anatomy The Jikei University School Of Medicine
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Fukushima Osamu
Department Of Anatomy (i) The Jikei University School Of Medicine
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