Results 11 to 20 of about 20,636 (170)

Characterization and Comparison of Milk Fat Globule Membrane Proteins, Whey Protein Concentrate, and Micellar Casein Concentrate. [PDF]

open access: yesFood Sci Nutr
This study compared milk fat globule membrane protein (MFGMP) with whey protein concentrate (WPC) and micellar casein concentrate (MCC). The results revealed MFGMP's superior structural stability and amino acid profile, identified its unique proteomic landscape through label‐free quantification, and demonstrated its enhanced in vitro digestibility ...
Wang J   +6 more
europepmc   +2 more sources

OmpA_C-Like Domain of PorE Is Essential for PorE Function in the Type IX Secretion System (T9SS) of Porphyromonas gingivalis and Some T9SS Cargo Proteins Are Secreted in a PorE-Independent Manner. [PDF]

open access: yesMicrobiol Immunol
ABSTRACT The periodontal pathogen Porphyromonas gingivalis secretes gingipains, highly hydrolytic proteases, to the cell surface or external environment via a type IX secretion system (T9SS). PorE is one of the T9SS component proteins essential for gingipain secretion. It consists of four domains: TPR, WD40, CRD, and OmpA_C‐like.
Tominaga T   +9 more
europepmc   +2 more sources

A Drosophila pattern recognition receptor contains a peptidoglycan docking groove and unusual L,D-carboxypeptidase activity.

open access: yesPLoS Biology, 2004
The Drosophila peptidoglycan recognition protein SA (PGRP-SA) is critically involved in sensing bacterial infection and activating the Toll signaling pathway, which induces the expression of specific antimicrobial peptide genes.
Chung-I Chang   +7 more
doaj   +1 more source

Advanced Glycation End Products of Bovine Serum Albumin Suppressed Th1/Th2 Cytokine but Enhanced Monocyte IL-6 Gene Expression via MAPK-ERK and MyD88 Transduced NF-κB p50 Signaling Pathways

open access: yesMolecules, 2019
Advanced glycation end products (AGE), the most known aging biomarker, may cause “inflamm-aging” (i.e., chronic low-grade inflammation that develops with aging) in both aged and diabetes groups.
Chieh-Yu Shen   +6 more
doaj   +1 more source

Digestive proteolytic activity in Apodiphus amygdali Germar (Hemiptera: Pentatomidae): effect of endogenous inhibitors

open access: yesJournal of Entomological and Acarological Research, 2014
The digestive proteolytic profile of Apodiphus amygdali was determined by using several substrates and specific inhibitors. Analysis of optimal pH and temperature showed the highest enzymatic activity at the pH range of 6-7 and temperature of 40°C when ...
S. Ramzi, A. Zibaee
doaj   +1 more source

Lysine Biosynthesis in Bacteria: A Metallodesuccinylase as a Potential Antimicrobial Target [PDF]

open access: yes, 2012
In this review, we summarize the recent literature on dapE-encoded N-succinyl-l,l-diaminopimelic acid desuccinylase (DapE) enzymes, with an emphasis on structure–function studies that provide insight into the catalytic mechanism.
Becker, Daniel P.   +2 more
core   +2 more sources

Inhibition of plasminogen activation by apo(a): role of carboxyl-terminal lysines and identification of inhibitory domains in apo(a)[S]

open access: yesJournal of Lipid Research, 2014
Apo(a), the distinguishing protein component of lipoprotein(a) [Lp(a)], exhibits sequence similarity to plasminogen and can inhibit binding of plasminogen to cell surfaces. Plasmin generated on the surface of vascular cells plays a role in cell migration
Rocco Romagnuolo   +3 more
doaj   +1 more source

High expression of human carboxypeptidase M in Pichia pastoris: Purification and partial characterization

open access: yesBrazilian Journal of Medical and Biological Research, 2006
Carboxypeptidase M (CPM) is an extracellular glycosylphosphatidyl-inositol-anchored membrane glycoprotein, which removes the C-terminal basic residues, lysine and arginine, from peptides and proteins at neutral pH.
R.B. Craveiro   +7 more
doaj   +1 more source

Carboxypeptidase M Expressed by Human Bone Marrow Cells Cleaves the C-Terminal Lysine of Stromal Cell-Derived Factor-1α: Another Player in Hematopoietic Stem/Progenitor Cell Mobilization? [PDF]

open access: yesStem Cells, 2008
Abstract Carboxypeptidase M (CPM) is a membrane-bound zinc-dependent protease that cleaves C-terminal basic residues, such as arginine or lysine, from peptides/proteins. We examined whether CPM is expressed by hematopoietic and stromal cells and could degrade stromal cell-derived factor (SDF)-1α, a potent chemoattractant for ...
Marquez-Curtis, Leah   +5 more
openaire   +3 more sources

Peptide inhibitors of Streptomyces DD-carboxypeptidases [PDF]

open access: yes, 1973
1. Peptides that inhibit the dd-carboxypeptidases from Streptomyces strains albus G and R61 were synthesized. They are close analogues of the substrates of these enzymes.
Frère, Jean-Marie   +4 more
core   +1 more source

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