(Q24315717)

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The hemoregulatory peptide N-acetyl-Ser-Asp-Lys-Pro is a natural and specific substrate of the N-terminal active site of human angiotensin-converting enzyme

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scholarly article

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The hemoregulatory peptide N-acetyl-Ser-Asp-Lys-Pro is a natural and specific substrate of the N-terminal active site of human angiotensin-converting enzyme (English)

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angiotensin I converting enzyme

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GOA release 2020-03-11

regulation of hematopoietic stem cell proliferation

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GOA release 2020-03-11

5

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author name string

A Rousseau

1

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A Michaud

2

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M T Chauvet

3

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M Lenfant

4

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language of work or name

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publication date

24 February 1995

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Journal of Biological Chemistry

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270

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3656-61

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8

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A fluorogenic substrate for angiotensin-converting enzyme

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Kinetic properties of pulmonary angiotensin-converting enzyme. Hydrolysis of hippurylglycylglycine

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A dipeptidyl carboxypeptidase that converts angiotensin I and inactivates bradykinin

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Negative regulator of pluripotent hematopoietic stem cell proliferation in human white blood cells and plasma as analysed by enzyme immunoassay

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Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung

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The testicular transcript of the angiotensin I-converting enzyme encodes for the ancestral, non-duplicated form of the enzyme

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Angiotensin converting enzyme: Implications from molecular biology for its physiological functions

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Anion activation of angiotensin converting enzyme: dependence on nature of substrate

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Catalysis of angiotensin I hydrolysis by human angiotensin-converting enzyme: effect of chloride and pH

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Electrophoretic Mobilities of Peptides on Paper and their Use in the Determination of Amide Groups

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Angiotensin I-converting enzyme in human circulating mononuclear cells: genetic polymorphism of expression in T-lymphocytes

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Involvement of human plasma angiotensin I-converting enzyme in the degradation of the haemoregulatory peptide N-acetyl-seryl-aspartyl-lysyl-proline

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Novel activity of human angiotensin I converting enzyme: release of the NH2- and COOH-terminal tripeptides from the luteinizing hormone-releasing hormone

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Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning

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Molecular cloning of human testicular angiotensin-converting enzyme: the testis isozyme is identical to the C-terminal half of endothelial angiotensin-converting enzyme

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The preparation and function of the hypertensin-converting enzyme

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The mechanism of action of the tetrapeptide acetyl-N-Ser-Asp-Lys-Pro (AcSDKP) in the control of haematopoietic stem cell proliferation

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Amelioration of chemotherapy-induced toxicity by cotreatment with AcSDKP, a tetrapeptide inhibitor of hematopoietic stem cell proliferation

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Angiotensin I converting enzyme and the changes in our concepts through the years. Lewis K. Dahl memorial lecture

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