Intermediate complex of ATP hydrolysis and synthesis by muscle proteins
β Scribed by Hotta, K.
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1975
- Tongue
- English
- Weight
- 240 KB
- Volume
- 3
- Category
- Article
- ISSN
- 0091-7419
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β¦ Synopsis
Abstract
Myosin catalyzed exchange between ^32^P~i~ and ATP in reaction medium during its enzymatic hydrolysis of ATP only by a very small amount. Addition of actin increased to a great extent the rate of incorporation of ^32^P~i~ in the presence of Mg. Glycerinated smooth muscle fibers also exhibited the ability to exchange ^32^P~i~ and ATP upon the application of external force (repeated stretching and releasing). A schematic mechanism of the action of actin and external force on acceleration of ^32^P~i~ incorporation is proposed and the importance of the M*βADP complex for force generation is suggested.
π SIMILAR VOLUMES
ATPase was detected in the membranes of a motile Streptococcus. Maximal enzymic activity was observed at pH 8 and ATP/Mg 2 Β§ ratio of 2. Mn 2 + and Ca 2 Β§ could replace Mg 2 + to some extent. Besides ATP, GTP and ITP were substrates. The enzyme was inhibited by N,N'-dicyclohexylcarbodiimide but not
## Protein degradation in animal and bacterial cells is dependent upon ATP [ 1,2]. In bacteria [3-61 and mammalian mitochondria [7], this energy dependence arises in large part from the involvement of a novel type of proteinase whose function is directly coupled to ATP hydrolysis [2,3]. The best-c