Results 131 to 140 of about 20,636 (170)

Structure of the microbial carboxypeptidase T complexed with the transition state analog N-sulfamoyl-l-lysine

Biophysical Chemistry, 2021
Carboxypeptidase T (CPT) from Thermoactinomyces vulgaris (EC 3.4.17.18) has a broad substrate specificity, the mechanism of which remains unclear. It cleaves off arginine residues by 10, and lysine residues by 100 times worse than hydrophobic leucine residues despite the presence of negatively charged Asp260 at the bottom of the primary specificity ...
Valery Kh, Akparov, Galina E, Konstantinova, Vladimir I, Timofeev, Ilyas G, Khaliullin, Inna P, Kuranova   +4 more
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Effect of Nepsilon-alkylation of the substrate on the hydrolysis of benzoylglycyl-L-lysine by carboxypeptidase B1.

Canadian journal of biochemistry, 1976
The action of carboxypeptidase B (EC 3.4.12.3) on the benzoylglycyl dipeptides Bz-Gly-Lys(X) where X = methyl, ethyl, propyl, formyl, dimethyl, isopropyl, trimethyl, and benzyl has been investigated. All were hydrolyzed, at a rate decreasing in the order indicated, except where X = trimethyl and benzyl.
G J, Moore, N L, Benoiton
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BLOCKAGE OF PROTEIN ENZYMATIC DIGESTION (CARBOXYPEPTIDASE‐B) BY HEAT‐INDUCED SUGAR‐LYSINE REACTIONS

Journal of Food Science, 1979
ABSTRACT TO investigate heat‐induced sugar‐lysine reactions in proteins (Mail‐lard browning) solutions of glucose and poly‐L‐lysine (lysine glucose ratio 1:l) were heated at selected temperatures (101—170° C) as a function of time. Spectra of such solutions exhibit absorbance maxima at 287 nm and 330 nm.
L. P. HANSEN, R. J. MILLINGTON
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HDAC1 regulates the stability of glutamate carboxypeptidase II protein by modulating acetylation status of lysine 479 residue

Biochemical and Biophysical Research Communications, 2018
Our previous study showed that the level of glutamate carboxypeptidase II (GCPII) protein is regulated by valproic acid, a histone deacetylase (HDAC) inhibitor, through acetylation of lysine residue in the GCPII protein in human astrocytes, U-87MG. The present study further investigated which HDAC subtype is involved in the acetylation of GCPII.
Ji-Young Choi, Jun-Hyeok Ko, Sangmee Ahn Jo   +2 more
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The carboxypeptidase B-catalyzed hydrolysis of poly-ϵ-N-methyl-L-lysine and poly-ϵ-N, ϵ-N-dimethyl-L-lysine

Biochemical and Biophysical Research Communications, 1969
Abstract Poly-ϵ- N -methyl-L-lysine was hydrolyzed by porcine carboxypeptidase B at a rate comparable with that for the hydrolysis of poly-L-lysine.Poly-ϵ-N, ϵ-N-dimethyl-L-lysine was hydrolyzed, but at a slower rate. All three curves describing the release of free amino acid are characterized by an initial rate lasting one hour followed by a ...
John H. Seely, N. Leo Benoiton
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Rapid assay of human plasma carboxypeptidase N by high-performance liquid chromatographic separation of hippuryl-lysine and its product

Journal of Chromatography A, 1983
A rapid and sensitive method for measuring carboxypeptidase N (CPN) activity in human plasma is described. The procedure is based on the hydrolysis of a high-specificity/low-affinity substrate, hippuryl-L-lysine, to its products hippuric acid and lysine. The substrate and product are separated quantitatively by high-performance liquid chromatography in
F, Marceau, A, Drumheller, M, Gendreau, A, Lussier, S, St-Pierre   +4 more
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Carboxypeptidase D is the only enzyme responsible for antibody C‐terminal lysine cleavage in Chinese hamster ovary (CHO) cells

Biotechnology and Bioengineering, 2016
ABSTRACTHeterogeneity of C‐terminal lysine levels often observed in therapeutic monoclonal antibodies is believed to result from the proteolysis by endogenous carboxypeptidase(s) during cell culture production. Identifying the responsible carboxypeptidase(s) for C‐terminal lysine cleavage in CHO cells would provide valuable insights for antibody ...
Zhilan, Hu, Henry, Zhang, Benjamin, Haley, Frank, Macchi, Feng, Yang, Shahram, Misaghi, Joseph, Elich, Renee, Yang, Yun, Tang, John C, Joly, Bradley R, Snedecor, Amy, Shen   +11 more
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Carboxypeptidase M Cleaves the C-Terminal Lysine of Stromal Cell-Derived Factor-1α and Is Expressed by Human Bone Marrow Cells.

Blood, 2006
Abstract Carboxypeptidase M (CPM) is a zinc-dependent phospho-inositol-anchored protease that cleaves carboxy-terminal basic residues such as arginine or lysine from peptides. CPM is primarily membrane-bound, glycosylated, has a neutral pH optimum, and occurs in placental microvilli, seminal plasma, amniotic fluid, peripheral nerves ...
Leah A. Marquez-Curtis, Kathleen Deiteren, Lambeir Anne-Marie, Ali Jalili, Neeta Shirvaikar, Anna Janowska-Wieczorek   +5 more
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Arginine and lysine product inhibition of bovine adrenomedullary carboxypeptidase H, a prohormone processing enzyme

Life Sciences, 1990
Carboxypeptidase H (CPH) is one of the later enzymes in the cascade of proteolytic steps required for the posttranslational processing of peptide hormone precursors, including processing of proenkephalin. In this study, CPH activity in the soluble and membrane fractions of enkephalin-containing bovine chromaffin granules was competitively inhibited by ...
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Assays for Arginine/Lysine Carboxypeptidases: Carboxypeptidases H (E; Enkephalin Convertase), M, and N

1991
Publisher Summary This chapter describes assay methods for arginine/lysine carboxypeptidases. The most frequently employed assay for carboxypeptidase H utilizes a fluorescent substrate, either 5-dimethylaminonaphthalene-l-sulfonyl (dansyl; Dns)-Phe-Leu-Arg or Dns-Phe-Ala-Arg.
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