Myosin: Biosynthesis, Classes and Function-Original PDF

Myosin: Biosynthesis, Classes and Function-Original PDF

Login is required


If you are not our user, for invitation Click Here

Amazon Price $95


Size : 5.33 MB

This Book opens with a discussion on class I myosins, the most varied members of the myosin superfamily and a remarkable group of molecular motor proteins that move actin filaments and produce force. Class I myosin molecules have various physiological roles including maintenance of normal intestinal brush border structure, glucose homeostasis, glomerular filtration, immune function, and tumor promotion and suppression, and new studies are revealing that mutations may lead to diseases including cancer and kidney disease. Next, the book discusses muscle contractile function and its association with the activity of the protein complex actomyosin, in which myosin exhibits enzyme activity, namely the ability to hydrolyze ATP. Following this, the authors present the results of their experiments on studying the effects of different isotopes of magnesium and zinc on the enzymatic activity of myosin, namely the catalytic subfragment-1 of myosin, isolated from myometrium muscle. It has been revealed that the rate of the enzymatic ATP hydrolysis is 2-2.5 times higher in the reaction media enriched with the magnetic isotope, 25Mg, as compared to the activity of the same enzyme in the reaction media enriched with the nonmagnetic isotopes, 24Mg or 26Mg or MgCl2 of natural isotope abundance. Western-blot analysis using commercial monospecific anti-human Myo1c antibodies has shown that the molecular mass of this protein obtained from a blood serum of different human sources varied in between 46-48 kDa. Thus, the authors name the 46-48 kDa proteins revealed in a blood serum as a short form of the human unconventional myosin 1c (sMyo 1C). (Nova)

Product Details

  • Series: Cell Biology Research Progress
  • Paperback: 186 pages
  • Publisher: Nova Science Pub Inc (June 1, 2018)
  • Language: English
  • ISBN-10: 1536138177
  • ISBN-13: 978-1536138177