Christopher Alexander Bauer

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Kinetic constants are reported for alpha-chymotrypsin-, Streptomyces griseus protease 3 (SGP3)-, and elastase-catalyzed hydrolysis of a number of peptides. SGP3, like alpha-chymotrypsine, hydrolyzes most readily amide bonds whose immediate acyl group (P1) is a large, hydrophobic, amino acid residue. SGP3, however, has a broader specificity for P1 residues(More)
Kinetic constants are reported for alpha-chymotrypsin- and Streptomyces griseus protease 3 (SGP3)-catalyzed amide hydrolysis of a number of peptide amides of varying substrate chain length. alpha-Chymotrypsin, but not SGP3, will hydrolyze rapidly specific acetyl amino acid amides. SGP3-catalyzed, but not alpha-chymotrypsin-catalyzed, hydrolysis is greatly(More)
Thin films of Ni<sub>80</sub>Fe<sub>20</sub>, Fe<sub>3</sub>O<sub>4</sub>, as well as Ni<sub>80</sub>Fe<sub>20</sub>/Cr/Fe<sub>3</sub>O<sub>4</sub> spin valves, have been grown with and without magnetic fields applied during the deposition, and their magnetotransport properties have been studied at room temperature. The applied field induces an anisotropy(More)