Zobrazeno 1 - 10
of 48
pro vyhledávání: '"Raymond Shapira"'
Autor:
Taehoon Lee, Cameron Sullards, Joseph M. Kinkade, Lisa Sharling, William A. Edens, Raymond Shapira, J. David Lambeth, Guy M. Benian, Heather A. Edens, Xuexin Tang, Guangjie Cheng, Denise B. Flaherty
Publikováno v:
The Journal of Cell Biology
High molecular weight homologues of gp91phox, the superoxide-generating subunit of phagocyte nicotinamide adenine dinucleotide phosphate (NADPH)-oxidase, have been identified in human (h) and Caenorhabditis elegans (Ce), and are termed Duox for “du
Publikováno v:
Molecular Immunology. 19:665-670
Antibodies against the 19 amino acid encephalitogenic peptide )residues 68-88) of guinea pig myelin basic protein (GPBP) were raised in Lewis (Le) rats. Anti-peptide antibodies were isolated from immune ascitic fluids by affinity chromatography using
Publikováno v:
Analytical Biochemistry. 154:345-352
The conditions for tryptic digestion and subsequent peptide mapping of the ATP-dependent proteolysis cofactor ubiquitin and its derivatives are described. In aqueous solution, the native ubiquitin which is composed of 76 amino acids undergoes only a
Autor:
William C. Mobley, S. B. Thiele, Robert F. Kibler, M. R. Wilhelmi, A. Wallace, Raymond Shapira
Publikováno v:
Journal of Neurochemistry. 30:735-744
— The enzyme 2′,3′-cyclic nucleotide-3′-phosphohydrolase (CNP) has been assayed in fractions from a continuous sucrose density gradient zonal centrifugation of rabbit brain homogenates. Basic protein (BP) was also assayed by a radioimmunometh
Publikováno v:
Journal of Neurochemistry. 28:115-119
— In the Lewis rat, fragment 43–88 of the highly encephalitogenic guinea-pig basic protein has been previously shown to retain the full activity of the parent protein. In the present studies this fragment was subjected to controlled chymotryptic
Autor:
Stephen O. Pember, Joseph M. Kinkade, John K. Spitznagel, L E Martin, Raymond Shapira, Katherine C. Barnes
Publikováno v:
Biochemical and Biophysical Research Communications. 114:296-303
Myeloperoxidase (MPO), a characteristic enzyme of human polymorphonuclear neutrophils (PMN), is localized in specialized lysosomal or azurophilic granules, and can be resolved into three distinct forms (I, II, III) by ion-exchange chromatography. Gra
Publikováno v:
Journal of Neurochemistry. 50:69-74
Neuritic plaque core amyloid protein in Alzheimer's disease brain tissue was investigated for the extent of amino acid racemization. Long-lived human proteins exhibit racemization of certain amino acids over the course of a human lifetime. Purified c
Publikováno v:
Journal of Neurochemistry. 28:1051-1059
— Chromatography of myelin basic protein (BP) on carboxymethylcellulose gives a pattern of multiple components, of which three are major. Component 1 is considered the unmodified species of BP while component 2 has been found to be modified primari
Publikováno v:
Journal of Neurochemistry. 30:745-750
— Myelin basic protein was isolated from the brains of 7 multiple sclerosis and 5 control patients. When acid extracts of the delipidated brains were chromatographed on carboxymethylcellulose at alkaline pH the elution profiles were the same for th
Publikováno v:
Archives of Biochemistry and Biophysics. 221:391-403
Multiple forms of myeloperoxidase from normal human neutrophilic granulocytes obtained from a single donor can be resolved by carboxymethyl (CM)-cellulose ion-exchange column chromatography into three forms (I, II, and III) designated in order of elu