Results 121 to 130 of about 3,638 (161)

ADAM10, myelin-associated metalloendopeptidase

2004
The subject of this chapter is ADAM10, myelin-associated metalloendopeptidase. ADAM10 is a zinc-dependent metallo-endopeptidase with a C-terminal distintegrin domain. It is a homolog of adamalysin. As an α-secretase, it is protective against Alzheimer’s disease, cleaving the Aβ protein so that the damaging β-secretase cleavage is reduced.
Postina, Rolf, Fahrenholz, Falk
openaire   +2 more sources

The novel ADAMs-like microbial metalloendopeptidase

Russian Journal of Bioorganic Chemistry, 2012
Heterologous gene expression of extracellular minor metalloendopeptidase of Bacillus pumilus 3-19 in protease-deficient B. subtilis strain has been studied. The fraction of enzyme in total pool of B. pumilus 3-19 secreted proteases composes less than 8%.
Balaban N., Rudakova N., Sabirova A., Valeeva L., Sharipova M.   +4 more
openaire   +4 more sources

Inhibition of metalloendopeptidases by 2‐mercaptoacetyl‐dipeptides

European Journal of Biochemistry, 1983
A series of 2‐mercaptoacetyl‐dipeptides, a potential group of metalloendopeptidase inhibitors, has been synthesized by coupling the N‐hydroxysuccinimide ester of S‐acetyl‐2‐mercaptoacetic acid with hydrophobic dipeptide methyl ester hydrochlorides, followed by hydrolysis with NaOH in aqueous methanol and acidification with HCl.
S, Blumberg, Z, Tauber
openaire   +2 more sources

New metalloendopeptidase of Morganella morganii ZM

Russian Journal of Bioorganic Chemistry, 2014
Proteolytic activity which is inhibited in the presence of o-phenanthroline was found in M. morganii ZM. Intracellular proteases of M. morganii ZM unlimited split musculoskeletal actin in contrast to grimelysin. Several proteolitic proteins of M. morganii ZM cells were identified by zymography with gelatin. Metalloproteinase of M.
Zamaliutdinova N., Minnullina L., Sharipova M., Mardanova A.   +3 more
openaire   +4 more sources

Biological markers in pneumoconioses : plasma metalloendopeptidase and matrix metalloendopeptidase

1991
The design and validation ofbiomarkers can contribute significantly to early detection of biological effects and identification ofthose who are at risk ofcoal workers' pneumoconiosis (CWP). This research is designed to evaluate diflerent plasma metalloendopeptidase and metalloproteinase activities to estimate harmfui exposure in coalminers from ...
Porcher, Jean-Marc, El Nabout, R., Oberson, Dominique, Auburtin, Guy, Gillet, Chantal, Sebastien, Patrick, Lafuma, C.   +6 more
openaire   +2 more sources

Biochemical and Immunological Properties of a Membrane‐Bound Brain Metalloendopeptidase: Comparison with Thermolysin‐Like Kidney Neutral Metalloendopeptidase

Journal of Neurochemistry, 1984
Abstract: Membrane‐bound neutral metalloendopeptidase (“enkephalinase”) was purified from rabbit brain and compared with a homogeneous preparation of a similar enzyme (EC 3.4.24.11) isolated from rabbit kidney. The two enzymes had the same pH optimum and the same apparent molecular weight.
J, Almenoff, M, Orlowski
openaire   +2 more sources

Degradation of bradykinin by a metalloendopeptidase from Streptococcus pyogenes

Journal of Oral Biosciences, 2016
Streptococcus pyogenes secretes streptococcal pyrogenic exotoxin B (SpeB), which cleaves kininogen to liberate bradykinin. In addition, this bacterium also has cell-associated bradykinin-degrading activity. Here, we characterized the bradykinin-degrading enzyme produced by S.
Yoichi, Miyamoto, Takaaki, Akaike, Shigetada, Kawabata, Teruo, Akuta, Chiho, Taruki, Jun, Yoshitake, Shigeyuki, Hamada, Fusao, Ota, Hideo, Igarashi, Kentaro, Yoshimura, Ryutaro, Kamijo, Hiroshi, Maeda   +11 more
openaire   +2 more sources

Action of neutral metalloendopeptidase (“enkephalinase”) on β-endorphin

Neuropeptides, 1985
Human beta-endorphin was digested by neutral metalloendopeptidase from rabbit kidney and the products were isolated and identified. Based on the structure and yield of the fragments, the major cleavage sites were identified with the Leu17-Phe18, Gly3-Phe4, Pro13-Leu14 and Ile22-Ile23 peptide bonds of the beta-endorphin structure.
L, Gráf, A, Páldi, A, Patthy
openaire   +2 more sources

Substrate-related potent inhibitors of brain metalloendopeptidase

Biochemistry, 1988
Rat brain metalloendopeptidase (EC 3.4.24.15) generates Leu- and Met-enkephalin from several larger opioid peptides and is capable of degrading a number of neuropeptides. Substrate-related N-(1-carboxy-3-phenylpropyl) peptide derivatives were synthesized and tested for enzyme inhibition.
M, Orlowski, C, Michaud, C J, Molineaux
openaire   +2 more sources

Structure modeling of a metalloendopeptidase from Corynebacterium pseudotuberculosis

Computers in Biology and Medicine, 2012
Metalloendopeptidases are zinc-dependent hydrolases enzymes with many different roles in biological systems, ranging from remodeling conjunctive tissue to removing signaling sequences from nascent proteins. Here, we describe the three-dimensional structure of the metalloendopeptidase from Corynebacterium pseudotuberculosis generated by homology ...
Luis Guimarães, Natália F. Silva, Anderson Miyoshi, Maria P. C. Schneider, Artur Silva, Vasco Ariston de Carvalho Azevedo, Davi S. B. Brasil, Jerônimo Lameira, Cláudio Nahum Alves   +8 more
openaire   +2 more sources