homoserine and muramidase

homoserine has been researched along with muramidase in 3 studies

Research

Studies (3)

Timeframe	Studies, this research(%)	All Research%
pre-1990	3 (100.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	0 (0.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Bonavida, B	1
Gutfreund, H	1
Dunn, A; Eshdat, Y; Sharon, N	1

Reviews

1 review(s) available for homoserine and muramidase

Article	Year
Transients and relaxation kinetics of enzyme reactions. Annual review of biochemistry, 1971, Volume: 40 Topics: Alcohol Oxidoreductases; Animals; Aspartic Acid; Catalase; Chemical Phenomena; Chemistry, Physical; Chymotrypsin; Computers; Endopeptidases; Enzymes; Escherichia coli; Flavoproteins; Glutamate Dehydrogenase; Glyceraldehyde-3-Phosphate Dehydrogenases; Hemoglobins; Homoserine; Horses; Hot Temperature; Kinetics; L-Lactate Dehydrogenase; Liver; Macromolecular Substances; Mathematics; Models, Biological; Muramidase; Myoglobin; NAD; Pancreas; Papain; Peroxidases; Phosphoric Monoester Hydrolases; Phosphotransferases; Protein Binding; Protein Conformation; Ribonucleases; Spectrophotometry; Temperature	1971

Article

Year

Transients and relaxation kinetics of enzyme reactions.

Annual review of biochemistry, 1971, Volume: 40

Topics: Alcohol Oxidoreductases; Animals; Aspartic Acid; Catalase; Chemical Phenomena; Chemistry, Physical; Chymotrypsin; Computers; Endopeptidases; Enzymes; Escherichia coli; Flavoproteins; Glutamate Dehydrogenase; Glyceraldehyde-3-Phosphate Dehydrogenases; Hemoglobins; Homoserine; Horses; Hot Temperature; Kinetics; L-Lactate Dehydrogenase; Liver; Macromolecular Substances; Mathematics; Models, Biological; Muramidase; Myoglobin; NAD; Pancreas; Papain; Peroxidases; Phosphoric Monoester Hydrolases; Phosphotransferases; Protein Binding; Protein Conformation; Ribonucleases; Spectrophotometry; Temperature

1971

Other Studies

2 other study(ies) available for homoserine and muramidase

Article	Year
Structural basis for immune recognition of lysozymes. IV. Immunologically active peptide obtained by the action of cyanogen bromide on human lysozyme. Immunochemistry, 1971, Volume: 8, Issue:9 Topics: Amino Acids; Animals; Antibodies; Antigen-Antibody Reactions; Chromatography, Gel; Coliphages; Cyanides; Cyanogen Bromide; Dextrans; Disulfides; Epitopes; Formates; Homoserine; Humans; Iodine Isotopes; Lactones; Leukemia, Myeloid; Methionine; Muramidase; Peptides; Rabbits; Structure-Activity Relationship	1971
Chemical conversion of aspartic acid 52, a catalytic residue in hen egg-white lysozyme, to homoserine. Proceedings of the National Academy of Sciences of the United States of America, 1974, Volume: 71, Issue:5 Topics: Amino Acid Sequence; Animals; Aspartic Acid; Carbon Radioisotopes; Catalysis; Chemical Phenomena; Chemistry; Chickens; Esters; Homoserine; Hydrogen-Ion Concentration; Muramidase; Ovalbumin; Oxidation-Reduction; Spectrometry, Fluorescence; Structure-Activity Relationship; Tritium	1974

Article

Year

Structural basis for immune recognition of lysozymes. IV. Immunologically active peptide obtained by the action of cyanogen bromide on human lysozyme.

Immunochemistry, 1971, Volume: 8, Issue:9

Topics: Amino Acids; Animals; Antibodies; Antigen-Antibody Reactions; Chromatography, Gel; Coliphages; Cyanides; Cyanogen Bromide; Dextrans; Disulfides; Epitopes; Formates; Homoserine; Humans; Iodine Isotopes; Lactones; Leukemia, Myeloid; Methionine; Muramidase; Peptides; Rabbits; Structure-Activity Relationship

1971

Chemical conversion of aspartic acid 52, a catalytic residue in hen egg-white lysozyme, to homoserine.

Proceedings of the National Academy of Sciences of the United States of America, 1974, Volume: 71, Issue:5

Topics: Amino Acid Sequence; Animals; Aspartic Acid; Carbon Radioisotopes; Catalysis; Chemical Phenomena; Chemistry; Chickens; Esters; Homoserine; Hydrogen-Ion Concentration; Muramidase; Ovalbumin; Oxidation-Reduction; Spectrometry, Fluorescence; Structure-Activity Relationship; Tritium

1974