Zobrazeno 1 - 10
of 166
pro vyhledávání: '"H. Mattenheimer"'
Autor:
P. Slabke, J. E. Scherberich, K. Jung, D. Maruhn, H. Mattenheimer, Z. J. Simane, A. S. Bhargava, H. Grötsch
Publikováno v:
Urinary Enzymes ISBN: 9783642843150
Aminopeptidases (α-aminoacylpeptide hydrolases, EC 3.4.11) comprise a group of exopeptidases, which split single amino acids from the N-terminus of peptide chains. Two, namely the cytosolic (EC 3.4.11.1) and the microsomal forms (EC 3.4.11.2), are o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::224e37d46b4497e58271fcd71a403551
https://doi.org/10.1007/978-3-642-84313-6_8
https://doi.org/10.1007/978-3-642-84313-6_8
Autor:
U. Burchardt, H. Mattenheimer
Publikováno v:
Urinary Enzymes ISBN: 9783642843150
Although it is now undisputed that renal tissue is the main source of most enzymes in the urine, some other potential sources should be considered: blood plasma, blood cells, bacteria, epithelium of the urinary tract, and seminal fluid. A classificat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::963bc96171b9b30937f6e9f0f55faa22
https://doi.org/10.1007/978-3-642-84313-6_1
https://doi.org/10.1007/978-3-642-84313-6_1
Autor:
H. Mattenheimer, D. Maruhn
Publikováno v:
Urinary Enzymes ISBN: 9783642843150
Urine constitutes an unfavourable environment for enzymes that interferes with the quantitative measurement of enzyme excretion. In contrast to plasma enzymes, which are protected by a relatively stable “enzyme friendly” milieu in a closed system
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9aae1d49c09226b1465182cfb1ed6e82
https://doi.org/10.1007/978-3-642-84313-6_6
https://doi.org/10.1007/978-3-642-84313-6_6
Autor:
Hs. Nitschmann, H. Mattenheimer
Publikováno v:
Helvetica Chimica Acta. 38:687-698
The velocity of the spliting off of NPN (Non Protein Nitrogen soluble in 12% trichloroacetic acid) from cow milk casein by various proteolytic enzymes at 30° and at neutral pH has been investigated. The enzymes were crystalline pepsin, crystalline c
Autor:
H. Mattenheimer, K. Borner
Publikováno v:
Mikrochimica Acta. 47:916-921
Die Herstellung von Mikropipetten aus Polyathylen mit Volumina von 0,4 bis 10μl wird beschrieben. Die Pipetten sind einfacher auf ein bestimmtes Volumen zu eichen als Konstriktionspipetten gleicher Grosenordnung und haben mit durchschnittlich ±0,4%
Publikováno v:
Helvetica Chimica Acta. 35:1970-1983
The phosphatase activity of two technically prepared rennins and of crystallized rennin from Berridge was investigated. Casein, phosphopeptone from casein, and glycerophosphate were subjected to the action of these rennin preparations.
Autor:
R. Friedel, H. Mattenheimer
Publikováno v:
Fresenius' Zeitschrift für analytische Chemie. 252:204-209
Die Herkunft der Zellenzyme im normalen Blutserum ist unerklart. In einer vergleichenden Untersuchung der LDH-Isoenzyme im Blutserum und in 10 Organen von Mensch, Marmoset-Affe, Ratte und Maus wurde gepruft, welche Organe als wesentliche Quelle fur d
Publikováno v:
Nephron. 7:144-154
The activity of LDH, MDH, G1DH, GOT, GPT, and CA was measured in the glomeruli, proximal convolutions, distal convolutions, medullary rays, outer zone of the medulla, inner zone of the medulla, and pa
Autor:
H. Mattenheimer, Hendrina DeBruin
Publikováno v:
Enzymologia biologica et clinica. 4:65-83
Autor:
H. Mattenheimer, R. Friedel
Publikováno v:
Clinica Chimica Acta. 30:37-46
The release of metabolic enzymes from platelets during clotting of blood and the subsequent increase of enzyme activities in serum were studied in man, dog, rabbit and rat. The activities of enzymes were measured which are present in blood cells with