Chip28 acronym
WebAquaporin 1 (AQP-1) is a protein that in humans is encoded by the AQP1 gene.. AQP-1 is a widely expressed water channel, whose physiological function has been most thoroughly characterized in the kidney.It is found … WebSemiconductor Group 2 SLE 4418 SLE 4428 Pin Configurations (top view) SLE 4418/4428 comes out as a M2.2 wire-bonded module for embedding in plastic cards or as a die
Chip28 acronym
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WebJan 15, 1993 · The sites of water transport along the nephron are well characterized, but the molecular basis of renal water transport remains poorly understood. CHIP28 is a 28-kD … WebJan 1, 1993 · CHIP28 is an integral membrane protein that has been identified as the erythrocyte water channel and that is also expressed in the kidney. Antibodies against erythrocyte CHIP28 were used to ...
WebObviously, the CHIP28 protein was needed for the cell to be able to let water in – the first water channel was discovered. Agre renamed the protein aquaporin, “water pore”. Eight years later and jointly with other research teams he presented the first high-resolution images of the three-dimensional structure of this protein. WebCHIP28 stands for "channel-forming integral protein of 28kDa". Q: A: How to abbreviate "channel-forming integral protein of 28kDa"? "channel-forming integral protein of 28kDa" can be abbreviated as …
WebCHIP28 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. … The sites of … WebJan 15, 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 …
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.
WebThe CHIP28 protein is an abundant integral membrane protein in mammalian RBCs and renal proximal tubules and belongs to a family of membrane proteins with unknown functions. Oocytes from Xenopus laevis microinjected with in vitro-transcribed CHIP28 RNA exhibited increased osmotic water permeability; this was reversibly inhibited by mercuric ... dalf shopWebStudy with Quizlet and memorize flashcards containing terms like Using SDS gel electrophoresis to separate proteins, _____ proteins migrate the fastest in the gel and move farther away from the _____ because of their _____ charge. a) large; anode; negative b) large; cathode; negative c) small; anode; negative d) large; cathode; positive e) small; … bipartisan report reviewWebidentification of this protein, so-called “CHIP28,” as a water channel has led to the discovery of a large family of water channels and related proteins (reviewed in Ref. 7). This family was first named the MIP family (MIP proteins) as an acronym for the first cloned protein of this family, the major dal free wifiWebAug 5, 2024 · an abbreviation for CHannel-forming Integral Protein of 28 kDa relative molecular mass. CHIP-28 was purified from the We use cookies to enhance your … bipartisan redistricting committees in statesWebJan 5, 1993 · These studies demonstrated: (i) CHIP28 water channel activity is retained despite substitution of individual cysteines with serine; (ii) cysteine 189 is the Hg (2+)-sensitive residue; (iii) the subunits of the CHIP28 complex are individually active water pores; (iv) residue 189 is critical to proper processing of the CHIP28 protein. bipartisan reform actWebAug 25, 1992 · Purified CHIP28 from human RBCs was reconstituted into proteoliposomes in order to establish if CHIP28 is itself the functional unit of water channels and to characterize its physiological behavior. CHIP28 proteoliposomes exhibit Pf which is up to 50-fold above that of control liposomes, but permeability to urea and protons is not increased. dal for chapatibipartisan reform act of 2002 summary