WebThe coinjection of an antisense oligonucleotide for CHIP28 protein, at an assumed > 100-fold molar excess, with either cortex, medulla, or papilla mRNA reduced the expression of the water permeability by approximately 70, 100, and 30%, respectively. Exposure of the oocyte to cAMP for 1 h resulted in a further increase in Pf only in oocytes ... WebConsumer Hybrid Intelligent Products and Services. CHIPS. Clearing House for Interbank Payments. CHIPS. Clearinghouse House Interbank Payment System. CHIPS. Canadian Hearing Instruments Practitioners Society. CHIPS. Competitive Human Interactive Player …
(PDF) Localization of the CHIP28 water channel in rat …
WebDec 15, 1991 · CHIP28 is a 28-kDa integral membrane protein with similarities to membrane channels and is found in erythrocytes and renal tubules. A cDNA for CHIP28 was isolated from human fetal liver cDNA template by a three-step polymerase chain reaction (PCR) cloning strategy, starting with degenerate oligonucleotide primers corresponding to the N … WebMay 15, 1993 · The CHIP28 water channel is a major component of red cell and renal tubule membranes; however, its ontogeny and tissue distribution remain undefined. Three … fisher investments returns 2018
CHIP28 water channels are localized in constitutively water-permeable ...
WebJan 2, 1993 · CHIP28 is a 28-kD integral protein which was proposed to mediate transmembrane water movement in red cells and kidney (Preston, G. M., T. P. Carroll, W. B. Guggino, and P. Agre. 1992. Science [Wash. DC]. 256:385-387). To determine whether CHIP28 could account for renal epithelial water transport, we used specific polyclonal … WebNov 16, 1992 · The cDNA coding for the rat CHIP28 water channel was isolated from a kidney library. At the amino acid level, rat CHIP28 is 93 % identical to the recently … WebIn 1993 CHIP28 was renamed aquaporin 1. Looking in retrospect, asking the crucial question, when was the first water channel protein, aquaporin 1, discovered, a fair and clear cut answer would be: the first water channel protein, now called aquaporin 1, was identified or "seen" in situ in the human RBC membrane by Benga and coworkers in 1986. fisher investments returns 2020