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October 1, 1986Journal of Biological ChemistryOpen Access

S-adenosylhomocysteinase from rat liver. Amino acid sequences of the peptides containing active site cysteine residues modified by treatment with 5'-p-fluorosulfonylbenzoyladenosine.

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Authors

TGTadashi GomiPrefectural University of HiroshimaHOHiroshi OgawaYamaguchi UniversityMFM. FujiokaHokkaido University

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Cite This Study

Gomi et al. (1986) studied this question.

synapsesocial.com/papers/6a81e861909f34cd697771ddhttps://doi.org/10.1016/s0021-9258(18)67034-6
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Evidence for an essential histidine residue in S-adenosylhomocysteinase from rat liver1983 · 67 citations
  2. 2Adenosylhomocysteine hydrolase. Crystallization of the purified enzyme and its properties.1978 · 146 citations
  3. 3Inactivation of rat liver S-adenosylhomocysteinase by iodoacetamide1982 · 30 citations
  4. 4<i>S</i> -Adenosylhomocysteine hydrolase from human placenta. Affinity purification and characterization1985 · 53 citations
  5. 5S-Adenosylhomocysteine hydrolase from rat liver. Purification and some properties.1981 · 91 citations