A monoclonal antibody to kidney endopeptidase-24.11. Its application in immunoadsorbent purification of the enzyme and immunofluorescent microscopy of kidney and intestine.

Por Gee, N S, Matsas, R, Kenny, A J
Publicado em 1983

The metabolism of neuropeptides. The hydrolysis of peptides, including enkephalins, tachykinins and their analogues, by endopeptidase-24.11.

Por Matsas, R, Kenny, A J, Turner, A J
Publicado em 1984

Substance P and [Leu]enkephalin are hydrolyzed by an enzyme in pig caudate synaptic membranes that is identical with the endopeptidase of kidney microvilli.

Por Matsas, R, Fulcher, I S, Kenny, A J, Turner, A J
Publicado em 1983

The metabolism of neuropeptides. Endopeptidase-24.11 in human synaptic membrane preparations hydrolyses substance P.

Por Matsas, R, Rattray, M, Kenny, A J, Turner, A J
Publicado em 1985

Kidney neutral endopeptidase and the hydrolysis of enkephalin by synaptic membranes show similar sensitivity to inhibitors.

Por Fulcher, I S, Matsas, R, Turner, A J, Kenny, A J
Publicado em 1982

The metabolism of neuropeptides. Phase separation of synaptic membrane preparations with Triton X-114 reveals the presence of aminopeptidase N.

Por Matsas, R, Stephenson, S L, Hryszko, J, Kenny, A J, Turner, A J
Publicado em 1985

Purification of endopeptidase-24.11 ('enkephalinase') from pig brain by immunoadsorbent chromatography.

Por Relton, J M, Gee, N S, Matsas, R, Turner, A J, Kenny, A J
Publicado em 1983

Cloning, expression and localization of human BM88 shows that it maps to chromosome 11p15.5, a region implicated in Beckwith-Wiedemann syndrome and tumorigenesis.

Por Gaitanou, M, Buanne, P, Pappa, C, Georgopoulou, N, Mamalaki, A, Tirone, F, Matsas, R
Publicado em 2001

Antigenicity and conformational analysis of the Zn(2+)-binding sites of two Zn(2+)-metalloproteases: Leishmania gp63 and mammalian endopeptidase-24.11.

Por Soteriadou, K P, Tzinia, A K, Panou-Pamonis, E, Tsikaris, V, Sakarellos-Daitsiotis, M, Sakarellos, C, Papapoulou, Y, Matsas, R
Publicado em 1996