S. Springhorn

发表

Renaturation of enzymes after polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate.

S. Lacks, S. Springhorn, 1980, The Journal of biological chemistry.

Transformation of restriction endonuclease phenotype in Streptococcus pneumoniae

S. Lacks, B. Greenberg, S. Springhorn, 1982, Journal of bacteriology.

Nucleotide sequence of the Dpn II DNA methylase gene of Streptococcus pneumoniae and its relationship to the dam gene of Escherichia coli.

S. Lacks, B. Greenberg, T. Balganesh, 1985, Proceedings of the National Academy of Sciences of the United States of America.

Proteins encoded by the DpnII restriction gene cassette. Two methylases and an endonuclease.

S. Lacks, S. Springhorn, A. G. de la Campa, 1987, Journal of molecular biology.

DpnA, a methylase for single-strand DNA in the Dpn II restriction system, and its biological function.

S. Lacks, S. Cerritelli, S. Springhorn, 1989, Proceedings of the National Academy of Sciences of the United States of America.

Cloning in Streptococcus pneumoniae of the gene for DpnII DNA methylase

S. Lacks, S. Springhorn, 1984, Journal of bacteriology.

ADENOSINE TRIPHOSPHATE CLEAVAGE DURING THE G-ACTIN TO F-ACTIN TRANSFORMATION AND THE BINDING OF ADENOSINE DIPHOSPHATE TO F-ACTIN.

D. Koshland, M. Bárány, S. Springhorn, 1964, The Journal of biological chemistry.

Lethal and mutagenic actions of N-methyl-N'-nitro-N-nitrosoguanidine potentiated by oxidized glutathione, a seemingly harmless substance in the cellular environment

S. Lacks, S. Springhorn, K. Kumaresan, 1995, Journal of bacteriology.

environment . seemingly harmless substance in the cellular potentiated by oxidized glutathione , a N-methyl-N '-nitro-N-nitrosoguanidine Lethal and mutagenic actions of

S. Lacks, S. Springhorn, K. Kumaresan, 1995 .

Effect of the composition of sodium dodecyl sulfate preparations on the renaturation of enzymes after polyacrylamide gel electrophoresis.

S. Lacks, S. Springhorn, A. L. Rosenthal, 1979, Analytical biochemistry.

Crystal structure of the DpnM DNA adenine methyltransferase from the DpnII restriction system of streptococcus pneumoniae bound to S-adenosylmethionine.

S. Lacks, S. Cerritelli, S. Springhorn, 1998, Structure.

Mechanism of action of 5'-nucleotidase.

D. Koshland, S. Springhorn, 1956, The Journal of biological chemistry.

Genetic basis of the complementary Dpnl and Dpnll restriction systems of S. pneumoniae: An intercellular cassette mechanism

S. Lacks, B. Greenberg, S. Springhorn, 1986, Cell.

Cleavage point during hydrolyses catalyzed by ribonuclease and phosphodiesterase.

D. Koshland, L. Heppel, S. Springhorn, 1961, Biochimica et biophysica acta.

Transfer of recombinant plasmids containing the gene for DpnII DNA methylase into strains of Streptococcus pneumoniae that produce DpnI or DpnII restriction endonucleases

S. Lacks, S. Springhorn, 1984, Journal of bacteriology.

Further evidence for oxygen exchange at an intermediate stage in myosin hydrolysis.

D. Koshland, S. Springhorn, H. M. Levy, 1962, The Journal of biological chemistry.

Identification of the histidine residue at the active center of trypsin labelled by TLCK.

E. Shaw, S. Springhorn, 1967, Biochemical and biophysical research communications.

Inactivation of boar acrosin by peptidyl-arginyl-chloromethanes. Comparison of the reactivity of acrosin, trypsin and thrombin.

E. Shaw, C. Kettner, S. Springhorn, 1978, Hoppe-Seyler's Zeitschrift fur physiologische Chemie.