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William J. Dreyer

Bio: William J. Dreyer is an academic researcher from United States Public Health Service. The author has contributed to research in topics: Bottom-up proteomics & Two-dimensional chromatography. The author has an hindex of 1, co-authored 1 publications receiving 658 citations.

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Journal ArticleDOI
TL;DR: The separation of peptides from controlled proteolytic digests by two-dimensional paper chromatography and electrophoresis is finding wide application to studies of protein structure.

658 citations


Cited by
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Journal ArticleDOI
TL;DR: Present evidence indicates that ly sozyme is the principal, if not the sole, product of the proliferating monocytes in monocytic and monomyelocytic leukemia, and quantitation of serum and urine lysozyme should be a useful diagnostic procedure for these leukemias.
Abstract: Markedly increased quantities of lysozyme have been found in the serum and urine (ranging to 2.6 g per day) of ten consecutive cases of monocytic and monomyelocytic leukemia. The enzyme has been isolated from the urine of several cases and physicochemically and immunochemically characterized. It is apparently identical to the lysozyme of normal tears, saliva, leukocytes, and serum, but structurally different from the lysozyme of hen's egg white. The activity of the human enzyme assayed with M. lysodeikticus organisms is 3 to 12 times greater than egg white lysozyme at equivalent concentrations. An agar plate method has been developed for quantitating lysozyme activity in small samples (approximately 25 µl) of serum, urine, or other biological fluids. The range and reproducibility of this method were found to be superior to previously available lysozyme assay procedures. Present evidence indicates that lysozyme is the principal, if not the sole, product of the proliferating monocytes in monocytic and monomyelocytic leukemia, and quantitation of serum and urine lysozyme should be a useful diagnostic procedure for these leukemias.

1,103 citations

Journal ArticleDOI
TL;DR: Analytical ultracentrifugation, amino acid analyses, manganese determination, and light-scattering measurements have been performed, and indicate that the E. coli enzyme exhibits marked specificity for the l isomer of glutamate.

565 citations

Journal ArticleDOI
TL;DR: The main virtues of the method are its speed, simplicity, and ability to handle crude extracts from small tissue samples, and willingness to handle tracer studies.

531 citations