Zobrazeno 1 - 10
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pro vyhledávání: '"W. B. Gratzer"'
Autor:
W. B. Gratzer, W. J. Brammar
Publikováno v:
Biographical Memoirs of Fellows of the Royal Society. 60:331-348
Sir Kenneth Murray—Ken to his friends—was held in high esteem and affection by all who knew him. In a remarkable career, which began after he left school at the age of 16 years, he played a prominent part, through his elegant and meticulous resea
Autor:
W. B. Gratzer, G. H. Beaven
Publikováno v:
International Journal of Peptide and Protein Research. 5:215-218
The introduction of intramolecular cross-links into trypsin with glutaraldehyde causes inactivation of the enzyme. When the reaction is performed in the presence of the inhibitor, benzamidine, a product of enhanced activity is obtained, although the
Publikováno v:
European Biophysics Journal. 28:208-215
We have examined the properties and interactions of expressed polypeptide fragments from the N-terminus of the alpha-chain and the C-terminus of the beta-chain of human erythroid spectrin. Each polypeptide comprises one complete structural repeating
Publikováno v:
Blood. 86:342-348
It is known that binding of extracellular antibodies against the major sialoglycoprotein, glycophorin A, reduced the deformability of the red blood cell membrane. This has been taken to result from new or altered interactions between the glycophorin
Publikováno v:
Biochemical Journal. 282:75-80
The intrinsic fluorescence of spectrin is strongly quenched by low concentrations of 2-bromostearate. This results from binding at a series of hydrophobic sites. Analysis of dynamic fluorescence quenching by acrylamide, iodide and caesium ions, separ
Publikováno v:
Journal of Biological Chemistry. 266:3835-3840
Spectrin chromatographically isolated from human red cell membranes contains a proteolytic activity, inhibited by leupeptin, with a dependence on calcium ions characteristic of a calpain I. The activity accompanies the spectrin on two successive gel
Autor:
Kevin C. Pedley, Wang Wei-dong, Magorzata Litwa, Jin Cheng-Zhi, Alison M. Maggs, G. H. Beaven, W. B. Gratzer
Publikováno v:
Molecular membrane biology. 14(3)
Fusion of human red cells through the action of polyethylene glycol gives rise to pairs or higher clusters with a common membrane envelope, in which a barrier at the position of the original interface can be seen in phase contrast. At early times thi
Publikováno v:
Cell motility and the cytoskeleton. 36(3)
We have prepared two fragments of the human dystrophin rod domain, each containing eight spectrin-like repeating units, by expression in Escherichia coli. The first corresponds to the central portion of the rod, the other to three repeats from the N-
Publikováno v:
Blood. 86(1)
It is known that binding of extracellular antibodies against the major sialoglycoprotein, glycophorin A, reduced the deformability of the red blood cell membrane. This has been taken to result from new or altered interactions between the glycophorin
Publikováno v:
Blood. 82(11)
The identity of the membrane binding sites for the membrane cytoskeletal protein 4.1 of the human red blood cell has been investigated. Exhaustive proteolysis of the membrane with a range of proteases led to the elimination of only some 60% of all bi