By Gerald Litwack
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Extra info for Biochemical Actions of Hormones. Volume 8
4 — — 54 45 Dedman et al. (1977b) Teo et al. (1973) — Values according to Watterson and Vanaman (1976). 6) 57 39 Lin et al. 3 — 20 40 20 Kuo and Coffee (1976) — — — Waisman et al. (1978) 1. 7 (J z < CÛ en O CO CÛ < 240 260 280 300 WAVELENGTH (nm) FIG. 5. Absorption spectra of earthworm modulator. 5 buffer containing 40 mM Tris/HCl, 1 mM MgAc2, and 50 μΜ CaCl2 was used. ) classes of binding sites appear to be present but there is no cooperativity in the binding of Ca2+ to these sites. y 1977). It appears that the structural and functional properties of calmodulin have been conserved phylogenetically.
The plasmalemma Ca2+ pumps of the human red blood cell and the canine heart microsomal pump have been well characterized and have been found to be regulated by calcium. 1 μΜ) to the extracellular fluid ([Ca2+] 1 mM) (Schatzmann and Vincenzi, 1969). The isolation of highly purified inside-out vesicles composed of plasma membrane has allowed characterization of the red blood cell Ca2+ pump. 8 μΜ has been reported by Waisman et ah (1980), a value in accordance with the physiological concentration of Ca2+ in these cells.
One class of light chain can be selectively removed from the myosin without loss of myosin ATPase activity and are referred to as the regulatory light chains (RLC). The other class, which are called the essential light chains (ELC), appear to be essential for myosin ATPase activity and cannot be removed without loss of enzymatic function. The presence of homologous RLC and ELC have been documented in the myosins of a variety of animals as well as in the myosin of nonmuscle contractile systems. In vertebrate smooth muscle and scallop adductor muscle it has been demonstrated that the RLC are responsible for the Ca2+-linked regulation of muscle contraction.
Biochemical Actions of Hormones. Volume 8 by Gerald Litwack