Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Betty H. Chao"'
Autor:
Stephen E. Fawell, Betty H. Chao, Gloria Chi-Rosso, Darren P. Baker, Kate Jiang, Leona E. Ling, Victor Koteliansky, Philip Gotwals, Linda C. Burkly, Jianliang Yang
Publikováno v:
Journal of Biological Chemistry. 272:31447-31452
Many cell-surface and extracellular matrix proteins contain multiple modular domains known as fibronectin type III (FNIII) repeats. Cells adhere to the extracellular matrix proteins fibronectin and tenascin in part by the interaction of certain integ
Autor:
Paula S. Hochman, Betty H. Chao, Cuervo Julio Hernan, Rem Baciu, Adrian Whitty, Margot Brickelmaier
Publikováno v:
Journal of immunological methods. 227(1-2)
Upon treatment with protein therapeutics, a subset of patients will typically develop antibodies against the drug. These anti-drug antibodies can be of concern because they have the potential to alter the drug's therapeutic activity. In the case of r
Publikováno v:
Biochemistry. 31(27)
Thrombin appears to activate platelets by a novel mechanism that involves the cleavage of its receptor, and it has been proposed that the newly generated N-terminal region of the receptor then acts as a tethered ligand [Vu, T. H., Hung, D. T., Wheato
Publikováno v:
FEBS letters. 294(3)
Using hirudin as a model, a novel class of bivalent thrombin inhibitors has been designed and characterized (Maraganore et al. (1990) Biochemistry 29, 7095–7101). These peptides, designated ‘hirulogs’, interact with both thrombin's catalytic ce
Publikováno v:
Journal of Biological Chemistry. 264:8692-8698
Synthetic peptides based on the COOH-terminal 21 residues of hirudin were prepared in order to 1) evaluate the role of this segment in hirudin action toward thrombin, 2) define the shortest peptide derivative with anticoagulant activity, and 3) inves
Autor:
Robert A. Fisher, Jeanne M. Bertonis, Patricia L. Chisholm, D S Costopoulos, C Williams, John M. Maraganore, Robert T. Schooley, J J Rosa, Tyler J. Curiel, Betty H. Chao
Publikováno v:
Journal of Biological Chemistry. 264:5812-5817
A gene encoding a 113-amino acid, NH2-terminal fragment of CD4, rsT4.113, was constructed and expressed in Escherichia coli under the control of the tryptophan operon promoter. Following induction, rsT4.113 is produced at 5-10% of total E. coli prote
Publikováno v:
Archives of Biochemistry and Biophysics. 226:643-656
The sequence of the bovine white matter proteolipid has been studied by a combination of proteolytic digestion and chemical cleavage at tryptophan residues. Alignment of peptides obtained by digestion with trypsin, chymotrypsin, clostripain, and Stap
Autor:
E P Chow, B Savage, U M Marzec, Betty H. Chao, Laurence A. Harker, John M. Maraganore, J A Jakubowski
Publikováno v:
Proceedings of the National Academy of Sciences. 86:8050-8054
Applaggin (Agkistrodon piscivorus piscivorus platelet aggregation inhibitor) is a potent inhibitor of platelet activation. The protein is isolated from the venom of the North American water moccasin snake in three steps, including gel filtration, cat
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 702:117-124
A hydrophobic, chloroform-soluble tryptic peptide with a molecular weight of approximately 4000 has been purified from the bovine white matter proteolipid protein. Its primary structure was obtained by a combination of solid-phase Edman degradation a
Publikováno v:
Neurochemical Research. 6:1091-1104
Bovine white matter proteolipid has been digested with elastase in the presence of deoxycholate. After acidification, the digest was separated into an acid-soluble and an acid-insoluble fraction. The acid-insoluble fraction was enriched in nonpolar a