Results 61 to 70 of about 4,028 (99)
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Degradation of lysylbradykinin by endopeptidase 24.11 and endopeptidase 24.15
Peptides, 1995Lysylbradykinin (LBK), a potent bioactive peptide with pleiotropic actions, is the major kinin generated in the extravascular space. To explore possible mechanisms of inactivation of this peptide in tissues, we evaluated its degradation by endopeptidase 24.11 (EP 24.11) and endopeptidase 24.15 (EP 24.15), two zinc metalloenzymes widely distributed in ...
Christopher Cardozo +3 more
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2013
In the course of solubilization and purification of fusicoccin binding sites present in microsomal fractions of spinach (Spinaciaoleracea L.)leaves,some endogenous hydrolases responsible for the poor stability of the receptors were identified [1]. Among them there was a serine proteinase displaying leucine-specific proteolytic activity.To reflect its ...
ADUCCI, PATRIZIA, Ascenzi, P.
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In the course of solubilization and purification of fusicoccin binding sites present in microsomal fractions of spinach (Spinaciaoleracea L.)leaves,some endogenous hydrolases responsible for the poor stability of the receptors were identified [1]. Among them there was a serine proteinase displaying leucine-specific proteolytic activity.To reflect its ...
ADUCCI, PATRIZIA, Ascenzi, P.
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Prolyl endopeptidase inhibitors
Il Farmaco, 2000Selective prolyl endopeptidase inhibitors were elaborated by modification of the structure of SUAM-1221, by using a CoMFA study and protein crystallography. The most active representatives of omega-(N-hetaryl)alkanoylprolylpyrrolidines, containing 2- or 3-methylene chain links have high activity (IC50 10(-9)-10(-11)) and exhibit significant in vivo ...
Károly Kánai, István Hermecz
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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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[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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