An endo-acting proline-specific oligopeptidase from Treponema denticola ATCC 35405: evidence of hydrolysis of human bioactive peptides. [electronic resource]
Producer: 19941122Description: 4938-47 p. digitalISSN:- 0019-9567
- Amino Acid Sequence
- Amino Acids -- analysis
- Angiotensin II -- metabolism
- Bradykinin -- metabolism
- Chelating Agents -- pharmacology
- Enzyme Activation -- drug effects
- Histidine
- Humans
- Hydrogen-Ion Concentration
- Kinetics
- Molecular Sequence Data
- Molecular Weight
- Oligopeptides -- metabolism
- Prolyl Oligopeptidases
- Sequence Alignment
- Sequence Homology, Amino Acid
- Serine
- Serine Endopeptidases -- chemistry
- Sodium Chloride -- pharmacology
- Structure-Activity Relationship
- Substance P -- metabolism
- Substrate Specificity
- Sulfhydryl Compounds -- pharmacology
- Temperature
- Treponema -- enzymology
- Vasopressins -- metabolism
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Publication Type: Comparative Study; Journal Article; Research Support, U.S. Gov't, P.H.S.
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