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J M Gleisner

Showing results (1-10 of 16) with videos related to

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Microbios|January 1, 1981
Characterization and comparison of aminopeptidase activity of various strains of Mycobacterium tuberculosisJ M Gleisner, C A Ramthun
Biochimica Et Biophysica Acta|December 17, 2009
Chemical modification of the histidine residue located at the active site of ficinJ M Gleisner, I E Liener
European Journal of Biochemistry|June 16, 1975
The structure of dihydrofolate reductase. Identification of methionine residues carboxymethylated by iodoacetate with loss of catalytic activityJ M Gleisner, R L Blakley
The Journal of Biological Chemistry|February 25, 1975
The structure of dihydrofolate reductase. I. Inactivation of bacterial dihydrofolate reductase concomitant with modification of a methionine residue at the active siteJ M Gleisner, R L Blakley
Respiration Physiology|December 1, 1986
Lung tissue tension and glycosaminoglycansJ M Gleisner, C J Martin
Inflammation|March 1, 1981
Inhibition of mast-cell degranulation by chemotactic peptidesJ M Gleisner, C A Ramthun, J C Houck
Inflammation|September 1, 1979
Macromolecular, anionic pulmonary permeability factorJ C Houck, J M Gleisner, C M Chang
The Journal of Biological Chemistry|July 10, 1975
The structure of the mutant dihydrofolate reductase from Streptococcus faecium. Partial sequence and order of the limited tryptic and cyanogen bromide peptidesJ M Gleisner, D L Peterson, R L Blakley
Biochemistry|December 2, 1975
Bovine liver dihydrofolate reductase: purification and properties of the enzymeD L Peterson, J M Gleisner, R L Blakley
The Journal of Biological Chemistry|July 10, 1975
The structure of the mutant dihydrofolate reductase from Streptococcus faecium. Amino acid sequence of peptide CNBr 7 and complete sequence of the proteinD L Peterson, J M Gleisner, R L Blakley
Pageof 2

Showing results (1-10 of 16) with videos related to

Sort By:
Pageof 2
Microbios|January 1, 1981
Characterization and comparison of aminopeptidase activity of various strains of Mycobacterium tuberculosisJ M Gleisner, C A Ramthun
Biochimica Et Biophysica Acta|December 17, 2009
Chemical modification of the histidine residue located at the active site of ficinJ M Gleisner, I E Liener
European Journal of Biochemistry|June 16, 1975
The structure of dihydrofolate reductase. Identification of methionine residues carboxymethylated by iodoacetate with loss of catalytic activityJ M Gleisner, R L Blakley
The Journal of Biological Chemistry|February 25, 1975
The structure of dihydrofolate reductase. I. Inactivation of bacterial dihydrofolate reductase concomitant with modification of a methionine residue at the active siteJ M Gleisner, R L Blakley
Respiration Physiology|December 1, 1986
Lung tissue tension and glycosaminoglycansJ M Gleisner, C J Martin
Inflammation|March 1, 1981
Inhibition of mast-cell degranulation by chemotactic peptidesJ M Gleisner, C A Ramthun, J C Houck
Inflammation|September 1, 1979
Macromolecular, anionic pulmonary permeability factorJ C Houck, J M Gleisner, C M Chang
The Journal of Biological Chemistry|July 10, 1975
The structure of the mutant dihydrofolate reductase from Streptococcus faecium. Partial sequence and order of the limited tryptic and cyanogen bromide peptidesJ M Gleisner, D L Peterson, R L Blakley
Biochemistry|December 2, 1975
Bovine liver dihydrofolate reductase: purification and properties of the enzymeD L Peterson, J M Gleisner, R L Blakley
The Journal of Biological Chemistry|July 10, 1975
The structure of the mutant dihydrofolate reductase from Streptococcus faecium. Amino acid sequence of peptide CNBr 7 and complete sequence of the proteinD L Peterson, J M Gleisner, R L Blakley
Pageof 2