Dr. Howard R Levy D.O.
Family Practitioner
5965 Chester Ave Philadelphia PA, 19143Rating
5/5
About
Dr. Howard Levy is a family practitioner practicing in Philadelphia, PA. Dr. Levy specializes in comprehensive health care for people of all ages. In addition to diagnosing and treating illnesses, family practitioners also put focus on preventative care with routine checkups, tests and personalized coaching on how to maintain a healthy lifestyle. Dr. Levy possesses immense general knowledge on maintaining health and today, family practitioners provide more care for the underserved and rural populations than any other medical specialty.
Provider Details
Expert Publications
Data provided by the National Library of Medicine- Fluorescent assay of anthranilate synthetase-anthranilate 5-phosphoribosylpyrophosphate phosphoribosyltransferase enzyme-complex on polyacrylamide gels.
- Anthranilate synthetase-anthranilate 5-phosphoribosylpyrophosphate phosphoribosyl-transferase from Salmonella typhimurium. Inactivation of glutamine-dependent anthranilate synthetase by agarose-bound anthranilate.
- An examination of the role of asp-177 in the His-Asp catalytic dyad of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase: X-ray structure and pH dependence of kinetic parameters of the D177N mutant enzyme.
- Delineation of the roles of amino acids involved in the catalytic functions of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase.
- NADP+ and NAD+ binding to the dual coenzyme specific enzyme Leuconostoc
- Glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides. Interaction of the enzyme with coenzymes and coenzyme analogs.
- Glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides. Interaction of the enzyme with coenzymes and coenzyme analogs.
- Lysine-21 of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase participates in substrate binding through charge-charge interaction.
- Protein turnover in growing cultures of Escherichia coli.
- The enzymatic transfer of hydrogen. V. The reaction catalyzed by glucose dehydrogenase.
- The enzymatic transfer of hydrogen. VI. The reaction catalyzed by D-glyceraldehyde-3-phosphate dehydrogenase.
- The stereospecificity of enzymatic hydrogen transfer from diphosphopyridine nucleotide.
- Bacterial oxidation of steroids. I. Ring A dehydrogenations by intact cells.
- Bacterial oxidation of steroids. II. Studies on the enzymatic mechanism of ring A dehydrogenation.
- The interaction of mammary glucose 6-phosphate dehydrogenase with pyridine nucleotides and 3beta-hydroxyandrost-5-en-17-one.
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