Abstract
A neutral brain endopeptidase which hydrolyzes bradykinin (Arg1-Pro2-Pro3-Gly4-Phe5-Ser6-Pro7-Phe8-Arg9) at the Phe5-Ser6 peptide bond was activated about 10 times by dithiothreitol. The preferential specificity of the enzyme for small peptides was suggested on the basis of the absence of activity toward a bradykinin-related protein such as S-carboxymethylated plasma kininogen.
MeSH terms
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Amino Acids / analysis
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Animals
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Bradykinin / metabolism*
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Brain / enzymology*
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Brain / ultrastructure
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Dithiothreitol / pharmacology
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Enzyme Activation / drug effects
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In Vitro Techniques
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Kininogens / metabolism*
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Peptide Hydrolases / metabolism*
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Peptides / analysis
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Rabbits
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Subcellular Fractions / enzymology
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Sulfhydryl Compounds / pharmacology*
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Time Factors
Substances
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Amino Acids
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Kininogens
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Peptides
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Sulfhydryl Compounds
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Peptide Hydrolases
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Bradykinin
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Dithiothreitol