mercaptoethanol and cytochrome c-t

mercaptoethanol has been researched along with cytochrome c-t in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	1 (50.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
MISAKA, E; MOTONAGA, K; NAKAJIMA, E; NAKANISHI, K; UEDA, S	1
Benson, DR; Cowley, AB; Lukat-Rodgers, GS; Rodgers, KR	1

Other Studies

2 other study(ies) available for mercaptoethanol and cytochrome c-t

Article	Year
STRUCTURE OF YEAST CYTOCHROME C. I. MONOMER AND DIMER INTERCONVERSION. Journal of biochemistry, 1965, Volume: 57 Topics: Ascorbic Acid; Benzoates; Chemical Phenomena; Chemistry; Chemistry Techniques, Analytical; Chemistry, Physical; Chloromercuribenzoates; Chromatography; Copper; Cytochromes; Cytochromes c; Electrophoresis; Mercaptoethanol; Molecular Weight; Radiometry; Research; Saccharomyces; Spectrophotometry; Sulfhydryl Compounds; Sulfites; Sulfur Isotopes	1965
A possible role for the covalent heme-protein linkage in cytochrome c revealed via comparison of N-acetylmicroperoxidase-8 and a synthetic, monohistidine-coordinated heme peptide. Biochemistry, 2004, Feb-17, Volume: 43, Issue:6 Topics: Animals; Binding Sites; Cytochromes c; Electron Spin Resonance Spectroscopy; Enzyme Stability; Ferric Compounds; Glycine; Heme; Hemeproteins; Histidine; Horses; Imidazoles; Iron; Ligands; Mercaptoethanol; Methionine; Peptide Fragments; Peptides; Protein Structure, Secondary; Spectrum Analysis, Raman; Structure-Activity Relationship	2004

Article

Year

STRUCTURE OF YEAST CYTOCHROME C. I. MONOMER AND DIMER INTERCONVERSION.

Journal of biochemistry, 1965, Volume: 57

Topics: Ascorbic Acid; Benzoates; Chemical Phenomena; Chemistry; Chemistry Techniques, Analytical; Chemistry, Physical; Chloromercuribenzoates; Chromatography; Copper; Cytochromes; Cytochromes c; Electrophoresis; Mercaptoethanol; Molecular Weight; Radiometry; Research; Saccharomyces; Spectrophotometry; Sulfhydryl Compounds; Sulfites; Sulfur Isotopes

1965

A possible role for the covalent heme-protein linkage in cytochrome c revealed via comparison of N-acetylmicroperoxidase-8 and a synthetic, monohistidine-coordinated heme peptide.

Biochemistry, 2004, Feb-17, Volume: 43, Issue:6

Topics: Animals; Binding Sites; Cytochromes c; Electron Spin Resonance Spectroscopy; Enzyme Stability; Ferric Compounds; Glycine; Heme; Hemeproteins; Histidine; Horses; Imidazoles; Iron; Ligands; Mercaptoethanol; Methionine; Peptide Fragments; Peptides; Protein Structure, Secondary; Spectrum Analysis, Raman; Structure-Activity Relationship

2004