Results 61 to 70 of about 3,066 (177)

Status quo and future developments in the diagnosis and treatment of hereditary angioedema

open access: yesJDDG: Journal der Deutschen Dermatologischen Gesellschaft, Volume 23, Issue 12, Page 1512-1525, December 2025.
Summary Hereditary angioedema (HAE) is a rare hereditary disease characterized by edema, which can be life‐threatening in case of swelling in the larynx. The most common form of HAE is caused by a mutation of the SERPING1 gene and is characterized by a deficiency (type I) or loss of function (type II) of the C1 inhibitor (C1‐INH), leading to excessive ...
Andreas Recke
wiley   +1 more source

Substitution of lysine 213 with arginine in penicillin-binding protein 5 of Escherichia coli abolishes D-alanine carboxypeptidase activity without affecting penicillin binding.

open access: yesJournal of Biological Chemistry, 1992
All penicillin-binding proteins (PBPs) contain a conserved box of homology in the carboxyl-terminal half of their primary sequence that can be Lys-Thr-Gly, Lys-Ser-Gly, or His-Thr-Gly. Site-saturation mutagenesis was used to address the role of the lysine residue at this position (Lys213) in Escherichia coli PBP 5, a D-alanine carboxypeptidase enzyme ...
K T, Malhotra, R A, Nicholas
openaire   +2 more sources

A study of aminopeptidases from lactic streptococci : a thesis presented in partial fulfilment of the requirements for the degree of Master of Science in Biochemistry at Massey University [PDF]

open access: yes, 1989
Two arninopeptidase enzymes from the proteolytic system of Streptococcus lactis 4760 have been studied. An X-Prolyl dipeptidyl arninopeptidase has been purified and characterised.
Lloyd, Richard John
core  

Met-Lys-bradykinin-Ser-Ser, a peptide produced by the neutrophil from kininogen, is metabolically activated by angiotensin converting enzyme in vascular tissue [PDF]

open access: yes, 2011
Bradykinin (BK) is a vasoactive nonapeptide cleaved from circulating kininogens and that is degraded by angiotensin converting enzyme (ACE). It has been reported that the PR3 protease from human neutrophil releases an alternate peptide of 13 amino acids,
Adam, Albert   +5 more
core   +1 more source

Purification and characterization of arginine-specific aminopeptidase and carboxypeptidase associated with cell membranes of Mycoplasma salivarium.

open access: yesJapanese Journal of Oral Biology, 1987
Mycoptasma salivariumのaminopeptidase (AP) およびcarboxypeptidase (CP) はともに細胞膜画分に局在していた。CPはTriton X-100で, そしてAPはその不溶性画分のpapain処理でそれぞれ可溶化され, 常法により精製された。精製されたAP (APM) は分子量が397-kilodalton (397K) で, discpolyacrylamide gel electrophoresis (disc-PAGE) でともに活性のある太いband (APMの90%に相当) と細いband (APMの5%に相当) をそれぞれ1本ずつ形成し, SDS-PAGEでは50Kと46Kのsubunit (1: 1, みかけのmolar ratio)
openaire   +2 more sources

Detection of peptidases in Trypanosoma cruzi epimastigotes using chromogenic and fluorogenic substrates [PDF]

open access: yes, 2017
Detergent extracts of Trypanosoma cruzi epimastigotes catalysed the hydrolysis of a range of amino-acyl and peptidyl p-nitro-anilides and aminomethylcoumarins. At least three enzymes were detected that cleave Z-Phe-Arg-MCA.
Ashall, F.   +6 more
core  

Kinetics and Identities of Extracellular Peptidases in Subsurface Sediments of the White Oak River Estuary, North Carolina [PDF]

open access: yes, 2019
Anoxic subsurface sediments contain communities of heterotrophic microorganisms that metabolize organic carbon at extraordinarily low rates. In order to assess the mechanisms by which subsurface microorganisms access detrital sedimentary organic matter ...
Alperin, Marc J.   +10 more
core   +2 more sources

Structure and activity of ChiX, a peptidoglycan hydrolase required for chitinase secretion by Serratia marcescens [PDF]

open access: yes, 2018
The Gram‐negative bacterium Serratia marcescens secretes a number of proteins that are involved in extracellular chitin degradation. This so‐called chitinolytic machinery includes three types of chitinase enzymes and a lytic polysaccharide monooxygenase.
Adam Lodge   +48 more
core   +2 more sources

Substrate Selectivity and Molecular Adaptation in the Outer Membrane Proteases of Yersinia pestis and Salmonella enterica [PDF]

open access: yes, 2010
Proteolysis is important in bacterial pathogenesis and colonization of animal and plant hosts. In this work I have investigated the functions of the bacterial outer membrane proteases, omptins, of Yersinia pestis and Salmonella enterica. Y.
Haiko, Johanna
core  

Functional characterization of the Mycobacterium tuberculosis zinc metallopeptidase Zmp1 and identification of potential substrates [PDF]

open access: yes, 2017
Zinc metallopeptidases of bacterial pathogens are widely distributed virulence factors and represent promising pharmacological targets. In this work, we have characterized Zmp1, a zinc metallopeptidase identified as a virulence factor of Mycobacterium ...
Amstutz, Beat   +11 more
core  

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