Results 31 to 40 of about 175,782 (300)

Cloning and heterologous expression of bovine pyroglutamyl peptidase type-1 in Escherichia coli : purification , biochemical and kinetic characterisation [PDF]

open access: yes, 2007
We describe the cloning, expression and purification of the bovine XM866409 form of pyroglutamyl-aminopeptidase I. The amino acid sequence, deduced from the nucleotide sequence, revealed that it consists of 209 amino acid residues and showed to have 98 ...
O'Connor, Brendan   +5 more
core   +2 more sources

Genome Wide Mapping of Peptidases in Rhodnius prolixus: Identification of Protease Gene Duplications, Horizontally Transferred Proteases and Analysis of Peptidase A1 Structures, with Considerations on Their Role in the Evolution of Hematophagy in Triatominae

open access: yesFrontiers in Physiology, 2017
Triatominae is a subfamily of the order Hemiptera whose species are able to feed in the vertebrate blood (i.e., hematophagy). This feeding behavior presents a great physiological challenge to insects, especially in Hemipteran species with a digestion ...
Bianca S. Henriques   +13 more
doaj   +1 more source

Seprase: An overview of an important matrix serine protease [PDF]

open access: yes, 2008
Seprase or Fibroblast Activation Protein (FAP) is an integral membrane serine peptidase, which has been shown to have gelatinase activity. Seprase has a dual function in tumour progression.
O\u27Brien, Pamela   +3 more
core   +2 more sources

Fusaoctaxin A, an Example of a Two-Step Mechanism for Non-Ribosomal Peptide Assembly and Maturation in Fungi

open access: yesToxins, 2019
Fungal non-ribosomal peptide synthetase (NRPS) clusters are spread across the chromosomes, where several modifying enzyme-encoding genes typically flank one NRPS.
Klaus Ringsborg Westphal   +10 more
doaj   +1 more source

Crystal structures of trypanosoma brucei oligopeptidase B broaden the paradigm of catalytic regulation in prolyl oligopeptidase family enzymes [PDF]

open access: yes, 2013
Oligopeptidase B cleaves after basic amino acids in peptides up to 30 residues. As a virulence factor in bacteria and trypanosomatid pathogens that is absent in higher eukaryotes, this is a promising drug target.
Rory E Morty   +15 more
core   +2 more sources

OPTIMIZATION OF PARAMETERS OF FERMENTOLYSIS OF PROTEINS IN THE COMPOSITION OF SERUM-PROTEIN CONCENTRATE

open access: yesHarčova Nauka ì Tehnologìâ, 2018
The food industry is a strategic industry that works quite steadily even during periods of economic crises, providing food security to any state, and is a source of raw material for other industries with a high potential for development, for example, for
N. Tkachenko   +4 more
doaj   +1 more source

A Multi-season Investigation of Microbial Extracellular Enzyme Activities in Two Temperate Coastal North Carolina Rivers: Evidence of Spatial but Not Seasonal Patterns

open access: yesFrontiers in Microbiology, 2017
Riverine systems are important sites for the production, transport, and transformation of organic matter. Much of the organic matter processing is carried out by heterotrophic microbial communities, whose activities may be spatially and temporally ...
Avery Bullock   +5 more
doaj   +1 more source

Molecular cloning and characterization of a novel peptidase from Trichinella spiralis and protective immunity elicited by the peptidase in BALB/c mice

open access: yesVeterinary Research, 2020
In our previous studies, a novel T. spiralis peptidase (TsP) was identified among the excretory/secretory (ES) proteins of T. spiralis intestinal infective larvae (IIL) and T.
Jun Jun Lei   +8 more
doaj   +1 more source

Kallikrein-related peptidase 15 (prostinogen) [PDF]

open access: yes, 2013
The third edition of the Handbook of Proteolytic Enzymes aims to be a comprehensive reference work for the enzymes that cleave proteins and peptides, and contains over 800 chapters. Each chapter is organized into sections describing the name and history,
Judith Clements   +3 more
core   +1 more source

Molecular characterisation of recombinant human pyroglutamyl peptidase (type I) [PDF]

open access: yes, 2005
Pyroglutamyl Peptidase I (PAP1, EC 3.4.19.3) hydrolytically cleaves pyroglutamic acid (pGlu) from the N-terminal of most pGlu-peptides. In higher organisms Thyrothropin Releasing Hormone is a notable biologically active substrate of PAP1. The sequence of
Vaas, Paul-Roman
core   +2 more sources

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