163 research outputs found
Sigma Nu Fraternity at UW front row L to R: Fred McCormick (1946), Tom Rosier (1946), Lou Colvin, Jack Henriot (1943), Larry Greene (1946), Gordy Woodland (1948), and Ced Tuohy (1944). Back row L to R: Jack McCarthy (1946), Mike Reeder (1946), Bob Ross (1946), Les Jones (1946).
Photo of Sigma Nu Fraternity at UW front row L to R: Fred McCormick (1946), Tom Rosier (1946), Lou Colvin, Jack Henriot (1943), Larry Greene (1946), Gordy Woodland (1948), and Ced Tuohy (1944). Back row L to R: Jack McCarthy (1946), Mike Reeder (1946), Bob Ross (1946), Les Jones (1946
A NOTE ON THE STOIGHIOMETRY OF ADSORPTION OF ANIONS BY LYSOZYME
Ten adsorbed anions of monovalent methyl orange, Orange II, or picric acid are necessary and sufficient to precipitate one lysozyme molecule at pH 5.5 in 0.05 M acetate buffer at 32°, whereas only five of divalent 2,4-dinitro-1-naphthol-7-sulphonic acid (flavianic acid) are required. These results are consistent with a hypothesis of interacting hydration effects. </jats:p
THE ADSORPTION OF METHYL ORANGE BY LYSOZYME
Adsorption isotherms for methyl orange on lysozyme at ionic strengths varying from 0.001 to 0.05, pH 5.5, are sigmoid. Increasing ionic strength shifts the inflection point of such isotherms to higher free anion concentrations. Binding of one methyl orange anion to a lysozyme molecule in 0.05 M acetate, pH 5.5, facilitates adsorption of nine others, with subsequent precipitation of the protein. This co-operative behavior is interpreted on the basis of a previously described theory of interacting hydration effects. The possible biological implications for similar systems are indicated. </jats:p
ADSORPTION OF ORANGE II BY CYTOCHROME <i>c</i> AND RIBONUCLEASE
The adsorption isotherms of Orange II on cytochrome c and ribonuclease at pH 5.5 in 0.05 M acetate buffer are sigmoid. They may be interpreted by a previously described theory of interacting hydration effects. Adsorption of methyl orange or sodium flavianate by either protein was negligible. </jats:p
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