Results 161 to 170 of about 32,233 (214)
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Pituitary endopeptidases

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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Proline-Specific Endopeptidases

Russian Journal of Bioorganic Chemistry, 2003
Prolyl endopeptidases, or post-proline-cleaving enzymes, are the specific endopeptidases that hydrolyze peptide substrates at the carbonyl of the internal Pro residue. All the currently known prolyl endopeptidases from animals, microorganisms, fungi, and plants as well as the post-proline-cleaving enzymes that do not exhibit the strict specificity to ...
D V, Besedin, G N, Rudenskaia
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Quantitation of Endopeptidase 24.11 and Endopeptidase 24.15 in Human Blood Leukocytes

Enzyme and Protein, 2017
Endopeptidase 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.
L, Casale   +3 more
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Biosynthesis of lysosomal endopeptidases

Journal of Cellular Biochemistry, 1989
AbstractDespite 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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PHEX Endopeptidase

2013
Mathieu St-Louis, Guy Boileau
openaire   +1 more source

O-Sialoglycoprotein endopeptidase

2004
Ping Jiang, Alan Mellors
openaire   +1 more source

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