P-type ATPases

Explain the mechanism of P-type ATPase; select P-type ATPase and examine how its physiological effects are studied. P-type ATPase is a large class membrane enzyme with 476 different subtypes that are classified in the Swiss-Prot protein information database. P-type or E1-E2 ATPase was first discovered by a Danish physician in 1957 and was classified as a physiologist Jens Christian Skou and later discovered Na + / K + ATPase and then in November 1997 the Nobel Prize in Chemistry Awarded. Works (Skou 1997).

The three first myosin isotypes identified were MHC I, MHCIIa and MHCIIb, which are isoforms I, IIA and IIB, respectively identified by myosin ATPase staining. 1, 3 and 5 respectively. Includes myosin. Thus, histochemical myosin ATPase type IC, IIC and IIAC fibers co-express MHCI and MHCIIa genes to varying degrees while IIAB fibers co-express "adjacent" (ie MHCI and MHCIIa or MHCIIa and MHCIIb) 2 . Co-expression of MHCIIa and MHCIIb genes 1 Because of its quantitative nature, the use of single-fiber electrophoretic separation (SDS-PAGE) to identify myosin heavy chain isoforms may be the best way for muscle fiber typing I do not. Electrophoretic separation allows detection of the relative concentrations of different myosin heavy chain isoforms in mixed fibers

This review explains the types of muscle fibers based on their histochemical, ultrastructural, biochemical, and physiological characteristics. Shrinkage of muscle fibers is directly proportional to relative myosin ATPase activity (pH 9.4) and fatigue has been reported to be related to relative oxidative capacity. Type I fibers have low ATPase activity (pH 9.4), slow contraction, high oxidizing power and low glycolysis, and are relatively resistant to fatigue. Type IIA fiber has high myosin ATPase activity (pH 9.4), rapid convulsion, high oxidation and glycolysis, and is relatively resistant to fatigue. Type IIB fiber has high myosin ATPase activity (pH 9.4), rapid convulsion, low oxidative and high glycolysis, and rapid fatigue