Soybean inhibitors. I. Separation and some properties of three inhibitors from commercial crude soybean trypsin inhibitor.
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Acrylic Resins↗
Biomedical subjects
R F Steiner
Publications and source records attributed to R F Steiner.
The phosphorescence of oligopeptides containing tryptophan and tyrosine.
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Glycols↗
The determination of association constants for a two-solute system. I. Colligative methods.
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Chemical Phenomena↗
The luminescence of tryptophan and phenylalanine derivatives.
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Dipeptides↗
The low temperature reaction of poly U and poly A.
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Adenine Nucleotides↗
Phosphorescence of soluble RNA.
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Adenine Nucleotides↗
The binding of thyroxine by serum albumin as measured by fluorescence quenching.
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Dialysis↗
Effects of pressure on the helix-coil transitions of the poly A-poly U system.
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Nucleic Acids↗
Accessibility and structural function of particular amino acid residues of soy bean trypsin inhibition.
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Chemical Phenomena↗
The alteration in the reactivity of the tyrosine and tryptophan groups of trypsin upon combination with protein inhibitors.
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Catalysis↗
The effect of environment on the structure and helix-coil transition of soluble ribonucleic acid.
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Chemical Phenomena↗
Fluorescent conjugates of biosynthetic polyribonucleotides.
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Acridines↗
Enzymically catalyzed disulfide interchange in randomly cross-linked soybean trypsin inhibitor.
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Animals↗
Properties of thyroglobulin. XII. Comparison of the configurational states of reduced and unreduced thyroglobulin.
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Fluorescence↗
The interaction of cyclosporin and calmodulin.
The interaction of cyclosporin A and dansyl cyclosporin A with bovine and wheat germ calmodulin has been monitored by measurements of induced changes in dansyl and bound toluidinyl naphthalene sulfonate fluorescence. The interaction is Ca2(+)-dependent and 1:1. Measurements of the efficiency of radiationless energy transfer from bound dansyl cyclosporin A to an acceptor group located on Cys-27 of wheat germ calmodulin suggest that the primary binding site is not located on the N-terminal lobe (residues 1-65). However, studies with proteolytic fragments of calmodulin indicate that elements of the N-terminal half-molecule (residues 1-77) may be involved in the stabilization of the binding site. The binding of cyclosporin alters the physical properties of calmodulin and, in particular, reduces the localized rotational mobility of a fluorescent probe.
Animals↗