Results 301 to 310 of about 82,787 (343)
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Life Sciences, 1983
Prolyl endopeptidase (E.C. 3.4.21.26) an enzyme previously called post proline cleaving enzyme, TRH-deamidase or kininase B, may play a role in neuropeptide metabolism. This enzyme, highly active in brain and other tissues, catabolizes proline-containing peptides such as substance P, neurotensin, luteinizing hormone-releasing hormone, thyrotropin ...
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Prolyl endopeptidase (E.C. 3.4.21.26) an enzyme previously called post proline cleaving enzyme, TRH-deamidase or kininase B, may play a role in neuropeptide metabolism. This enzyme, highly active in brain and other tissues, catabolizes proline-containing peptides such as substance P, neurotensin, luteinizing hormone-releasing hormone, thyrotropin ...
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Molecular and Cellular Biochemistry, 1983
This review summarizes our knowledge of pituitary endopeptidases. Emphasis has been placed on well-characterized enzymes and their potential roles in proteolytic processes of the pituitary. Because of space limitations, degradation of biologically active peptide by crude preparations has generally not been discussed.
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This review summarizes our knowledge of pituitary endopeptidases. Emphasis has been placed on well-characterized enzymes and their potential roles in proteolytic processes of the pituitary. Because of space limitations, degradation of biologically active peptide by crude preparations has generally not been discussed.
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Biosynthesis of lysosomal endopeptidases
Journal of Cellular Biochemistry, 1989AbstractDespite the clear differences between the amino acid sequence and enzymatic specificity of aspartic and cysteine endopeptidases, the biosynthetic processing of lysosomal members of these two families is very similar. With in vitro translation and pulse‐chase analysis in tissue culture cells, the biosynthesis of cathepsin D, a aspartic protease,
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Quantitation of Endopeptidase 24.11 and Endopeptidase 24.15 in Human Blood Leukocytes
Enzyme and Protein, 1994Endopeptidase 24.11 (EP 24.11; also called neutral endopeptidase, enkephalinase, CALLA, or CD10) and endopeptidase 24.15 (EP 24.15) are widely distributed neutral metalloendopeptidases that degrade a number of bioactive peptides including substance P, bradykinin, neurotensin, and chemotactic peptides.
Marvin Lesser +3 more
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2004
Publisher Summary This chapter elaborates the structural chemistry and the biological aspects of nodavirus endopeptidase. The chapter discusses that because the nodavirus endoprotease activity is associated with the precursor particle; a provirion preparation is required to study the protease activity.
Vijay Reddy +2 more
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Publisher Summary This chapter elaborates the structural chemistry and the biological aspects of nodavirus endopeptidase. The chapter discusses that because the nodavirus endoprotease activity is associated with the precursor particle; a provirion preparation is required to study the protease activity.
Vijay Reddy +2 more
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Neutral endopeptidase and alcohol consumption, experiments in neutral endopeptidase-deficient mice
European Journal of Pharmacology, 2000Alcohol consumption was investigated in mice which were rendered deficient in the peptide-degrading enzyme neutral endopeptidase (EC 3.4.24.11) (NEP-/-) by gene targeting and compared to alcohol consumption in corresponding wild type mice (NEP+/+). Mice were offered a free choice to drink tap water or 10% alcohol. The NEP-/- mice consumed significantly
Kurt F. Hauser +8 more
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[44] Isoprenylated protein endopeptidase
1994Publisher Summary This chapter highlights isoprenylated protein endopeptidases. In protein isoprenylation, a protein with a carboxyl terminal CX 3 or, much less frequently, a CXC or a CC(XX) sequence (where Cis cysteine, and X is an undefined amino acid) is first isoprenylated at the cysteine residues with either all- trans -farnesyl or all- trans -
Yu-Ting Ma, Robert R. Rando
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[38] Pineapple cysteine endopeptidases
1994Publisher Summary This chapter focuses on pineapple cysteine endopeptidases. The pineapple plant contains at least four distinct cysteine endopeptidases. The major endopeptidase present in extracts of plant stem is stem bromelain, and fruit bromelain is the major endopeptidase in the fruit. Two additional cysteine endopeptidases, ananain and comosain,
Andrew D Rowan, David J. Buttle
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2004
Publisher Summary This chapter discusses the structural chemistry and the biological aspects of endopeptidase germination proteinase (GPR). The discovery that 10%–20% of the protein of dormant spores of Bacillus species is rapidly degraded during spore germination led to the identification of GPR as the endopeptidase that initiates this proteolysis ...
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Publisher Summary This chapter discusses the structural chemistry and the biological aspects of endopeptidase germination proteinase (GPR). The discovery that 10%–20% of the protein of dormant spores of Bacillus species is rapidly degraded during spore germination led to the identification of GPR as the endopeptidase that initiates this proteolysis ...
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An endopeptidase of bean leaves
Canadian Journal of Botany, 1970Bean leaves yielded an enzyme which hydrolyzed casein and hemoglobin to large peptide fragments. The protease exhibited maximal activity at pH 9 to 10, an isoelectric point of 8.8, and a molecular weight of about 100 000. During leaf growth the protease increased in a manner suggestive of a developmental role in the control of protein content.
Murray Foote, David Racusen
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