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pmid: 14478317
Abstract The myosin ATP-ase us inhibited by ADP competitively. The inhibitation constant is 33 times the Michaelis constant. This small amount of inhibition explains the product versus time curve of the ATP hydrolysis and is confirmed by this curve. The association constant of CaAdp was determined as 1050. In order to establish true ADP inhibitiion Ca has to be in excess, so that Ca chelation by ADP does not affect Ca available to the myosin.
Adenosine Diphosphate, Adenosine Triphosphatases, Adenine Nucleotides, Muscle Proteins, Myosins
Adenosine Diphosphate, Adenosine Triphosphatases, Adenine Nucleotides, Muscle Proteins, Myosins
citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 31 | |
popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network. | Average | |
influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Top 1% | |
impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Top 10% |