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5 results on '"J.L. Hodnett"'

1. Tao-Chiuh Hsu

Author

M.W. Shaw, P.A. Shaw, S. Kit, D.A. Pepper, W. Au, J.L. Hodnett, C.E. Wilkins, G. Levan, E. Stubblefield, G.G. Maul, B.R. Brinkley, Harold P. Klinger, D. Rüedi, D.L. Robberson, H. Winking, M. McGill, M. Hazen, H. Qavi, G.A. King, A. Gropp, B.L. Maxwell, J. Kros, S.M. Cox, M.V. Marshall, J.J. Freed, Y.-F. Lau, S. Pathak, R.A. Pfeiffer, D.R. Dubbs, G.F. Saunders, R.R. Klevecz, L.L. Deaven, A.T. Kumamoto, A. Levan, C.H. Ockey, K. Nielsen, W. Beçak, H. Müller, F.E. Arrighi, O.I. Sokova, H.S. Downes, B. Kopnin, K.L. Wagner, F.F.B. Elder, Le M. Campbell, E.W. Campbell, D. Stehling, J.T. Mascarello, A. Spallone, Frances E. Arrighi, and Kurt Benirschke

Subjects
Genetics, Biology, Theology, Molecular Biology, Genetics (clinical)
Published
1980
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2. Isolation and partial characterization of supernatant and mitochondrial shrimp muscle malate dehydrogenases

Author

J.E. Evans, J.L. Hodnett, H.B. Gray, and A.H. Bartel

Subjects
Physiology, Malates, Dehydrogenase, Biochemistry, Malate dehydrogenase, Isozyme, Cytosol, Malate Dehydrogenase, Decapoda, biology.animal, Animals, Molecular Biology, chemistry.chemical_classification, Oxalates, biology, Molecular mass, Muscles, Vertebrate, General Medicine, Hydrogen-Ion Concentration, Molecular biology, Mitochondria, Muscle, Shrimp, Isoenzymes, Molecular Weight, Kinetics, Enzyme, chemistry, NAD+ kinase
Abstract

1. 1. The supernatant and mitochondrial forms of muscle malate dehydrogenase (E.C. 1.1.1.37) isolated from two closely related species of shrimp have molecular weights and hydrodynamic properties similar to those previously reported for the corresponding enzymes of vertebrates. 2. 2. The catalytic properties of these species more closely resemble those of the vertebrate malate dehydrogenases than those of lower eukaryotes. 3. 3. The electrophoretic behavior of the shrimp malate dehydrogenases indicates that they are comprised of two subunits. 4. 4. The subunits of the shrimp enzymes are non-identical and give rise to three electrophoretically distinguishable isoenzymes of each dehydrogenase.

Published
1976
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3. Contents, Vol. 26, 1980

Author

C.H. Ockey, R.R. Klevecz, L.L. Deaven, W. Au, R.A. Pfeiffer, F.E. Arrighi, D. Rüedi, D.L. Robberson, D.A. Pepper, J.T. Mascarello, P.A. Shaw, Harold P. Klinger, D.R. Dubbs, G.F. Saunders, M. McGill, D. Stehling, H. Qavi, J.L. Hodnett, J.J. Freed, B.L. Maxwell, K. Nielsen, C.E. Wilkins, S. Kit, A.T. Kumamoto, A. Levan, M.W. Shaw, S. Pathak, H.S. Downes, G.G. Maul, B. Kopnin, K.L. Wagner, B.R. Brinkley, G.A. King, E.W. Campbell, W. Beçak, A. Spallone, Le M. Campbell, Kurt Benirschke, Frances E. Arrighi, H. Winking, M. Hazen, E. Stubblefield, S.M. Cox, Y.-F. Lau, G. Levan, H. Müller, O.I. Sokova, A. Gropp, M.V. Marshall, F.F.B. Elder, and J. Kros

Subjects
Botany, Genetics, Biology, Molecular Biology, Genetics (clinical)
Published
1980
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4. A characterization of mitochondrial and mycoplasmal DNAs associated with cloned HeLa thymidine kinase minus cells

Author

D.L. Robberson, M.L. Gay, C.E. Wilkins, and J.L. Hodnett

Subjects
DNA, Bacterial, Mitochondrial DNA, EcoRI, HindIII, DNA, Mitochondrial, Thymidine Kinase, chemistry.chemical_compound, Mycoplasma, Genetics, Centrifugation, Density Gradient, Humans, Molecular Biology, Genetics (clinical), Electrophoresis, Agar Gel, biology, DNA Restriction Enzymes, Molecular biology, Restriction enzyme, Microscopy, Electron, chemistry, Bromodeoxyuridine, Thymidine kinase, Agarose gel electrophoresis, biology.protein, DNA, Circular, DNA, HeLa Cells
Abstract

HeLa S3 cells were cloned, recloned, and then selected for growth in the presence of increasing concentrations of bromodeoxyuridine. Cultures of these cloned thymidine kinase minus (TK-) cells were found to harbor mycoplasma which sedimented with mitochondria in sucrose density step gradients. Examination of mitochondrial DNA (mitDNA) components by restriction enzyme analysis and electron microscopy revealed no gross alterations in size, sequence arrangements, or replicative forms compared with mitDNA of HeLa S3 cells. Restriction enzyme cleavage sites for BamHl (one site), PstI (two sites) and HpaI (three sites) were mapped on this genome relative to the three cleavage sites for each of EcoRI and HindIII, respectively. Analysis of topological complexity revealed similar frequencies of catenated mitDNA molecules in both cloned TK– (22.5 ± 1.5% of mass) and HeLa S3 cells (25.6 ± 1.5% of mass). Unicircular dimers comprise 6.7 ± 0.9% of the mitDNA mass in cloned TK– cells but were not detected in HeLa S3 mitDNA. Examination of the mycoplasmal contaminant of mitochondrial DNA after digestion with various restriction enzymes and agarose gel electrophoresis revealed that most of the DNA was distributed in discretely sized fragments in patterns that can probably be used to unambiguously identify and classify the organism.

Published
1980

5. Subject Index Vol. 26, 1980

Author

H. Müller, C.E. Wilkins, O.I. Sokova, G.G. Maul, B.R. Brinkley, H. Winking, H.S. Downes, Y.-F. Lau, M. Hazen, D. Stehling, D. Rüedi, H. Qavi, Harold P. Klinger, B. Kopnin, M. McGill, G.A. King, K.L. Wagner, D.L. Robberson, G. Levan, K. Nielsen, B.L. Maxwell, W. Beçak, W. Au, J.T. Mascarello, S. Pathak, R.R. Klevecz, L.L. Deaven, S.M. Cox, F.E. Arrighi, J.J. Freed, E. Stubblefield, A. Gropp, M.V. Marshall, J. Kros, Le M. Campbell, E.W. Campbell, A. Spallone, M.W. Shaw, F.F.B. Elder, P.A. Shaw, J.L. Hodnett, D.A. Pepper, R.A. Pfeiffer, G.F. Saunders, D.R. Dubbs, A.T. Kumamoto, A. Levan, C.H. Ockey, S. Kit, Frances E. Arrighi, and Kurt Benirschke

Subjects
Index (economics), Statistics, Genetics, Subject (documents), Biology, Molecular Biology, Genetics (clinical)
Published
1980
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