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Excerpt from Treatise on traditional Philosophy, Vol. 2 An index to the full of the 1st quantity has been ready by means of Mr burnside, and is put on the finish. A time table is additionally given under of the entire amendments and additions (excepting in basic terms verbal alterations and corrections) made within the current version of the 1st quantity.
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Cell 39:49-59. Johnson, K. D. Lampe, K. C. Hur, C. F. Louis, and R. G. Johnson. 1986. A lens intercelluar junction protein, MP26 is a phosphoprotein. J. Cell Biol. 102:1334-1343. Lampe, P. D. Johnson. 1989. Phosphorylation of MP26, a lens junction protein, is enhanced by activators of protein kinase C. J. Membrane Biol. 107:145-155. D. Johnson. 1991. Amino acid sequence of in vivo phosphorylation sites in the main intrinsic protein (MIP) of lens membrane. Eur. J. Biochem. 194:541-547. Turnquist.
The most frequently observed calcium dependence of RyRl channels in bilayers was comparable to the calcium dependence of the release rate constants bilayers CALCIUM DEPENDENCE OF CALCIUM RELEASE CHANNELS 35 Cardiac Muscle Skeletal Muscle 1 10 Free [ C a 2 ! 1 1 10 Free [Ca2*], uM Figure 2. Calcium dependence of Ca2+ release rate constants from SR vesicles isolated from skeletal (A) and cardiac (B) muscle. Release kinetics were measured as described in the text. 2 and Calcium Green 5N for pCa < 6..
Water and non electrolyte fluxes follow the ionic currents, driven by small osmotic gradients generated by ion flow, and as material moves inward through extracellular space, a fraction enters the cells at each level and begins to flow in an outward direction (shown by arrows of decreasing size in the right-hand panel). Inside the cells, flow reverses direction and becomes outwardly directed. The driving energy for all this activity is thought to be generated by the Na-KATPase of the mitochondria-rich regions near the surface of the lens.