Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Pancreatic elastase II"'
Autor:
Dong-Eun Kim, Kwang Hyuk Kim, Woo Hong Joo, Jae Hyun Kim, Yong-Kee Jeong, Woong Suk Yang, Kyung Tae Chung, Jeong Uck Park
Publikováno v:
Biotechnology Letters. 26:393-397
A fibrinolytic enzyme, myulchikinase, from a Korean seasoning ingredient, myul-chi-jeot-gal, has been purified to electrophoretic homogeneity. The molecular mass of the myulchikinase was estimated to about 28 kDa by SDS-PAGE and gel filtration. Amino
Autor:
Diane H. Munzenmaier, Maria Cristina O. Salgado, Daniela Nicole Schippers, Eduardo B. Oliveira, Carlos Ferreira dos Santos, Andrew S. Greene, Marcos Antonio V. Caprio
Publikováno v:
American Journal of Physiology-Heart and Circulatory Physiology. 285:H775-H783
We recently described a chymostatin-sensitive elastase-2 as the major angiotensin (ANG) II-forming enzyme in the perfusate of the rat mesenteric arterial bed (MAB) with the same cDNA sequence as rat pancreatic elastase-2. The role of this enzyme in g
Publikováno v:
Journal of Protein Chemistry. 20:577-584
A peptidase (GICP) that cleaves the Gln-Ile bond of a peptide Gly-Ile-Asp-Val-Gln-Ile-Tyr(T-1), a sequence in phenylalanine oxidase, was purified from bovine pancreas. The purified enzyme had an Mr of approximately 29,000, as determined by SDS-PAGE,
Autor:
Jerry W. Skiles, Arco Y. Jeng
Publikováno v:
Expert Opinion on Therapeutic Patents. 9:869-895
The fibrous protein elastin, which comprises an appreciable percentage of all protein content in some tissues, such as arteries, some ligaments, and the lungs, can be hydrolysed or otherwise destroyed by a select group of enzymes classified as elasta
Autor:
I. Le Huërou-Luron, M. Gestin, A. Aumaitre, P. Guilloteau, E Thioulouse, J. Peiniau, D Feldman, G. Le Dréan, C. Desbois
Publikováno v:
Digestive Diseases and Sciences. 42:1302-1311
A specific method for pancreatic elastase II activity analysis was developed. True elastase II activity could be discriminated from that of elastase I and chymotrypsin. The postnatal development of four pancreatic proteases in the duodenal juice of c
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1251:55-65
A somatostatin-14-degrading activity has been purified to homogeneity from rat pure pancreatic juice. This proteinase was concentrated more than 350-fold in a four-step procedure including ion-exchange and gel filtration. The final preparation contai
Autor:
Dietmar Schomburg, Dörte Stephan
Publikováno v:
Enzyme Handbook 15 ISBN: 9783540641162
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0fff23001018a02aaf6b645188e8d702
https://doi.org/10.1007/978-3-642-58948-5_134
https://doi.org/10.1007/978-3-642-58948-5_134
Autor:
L. Roger, F. Mendy, T. Lengagne, C. Desbois, Paul Guilloteau, I. Le Huërou-Luron, Véronique Romé, G. Le Dréan, M. Gestin
Publikováno v:
Le Lait
Le Lait, INRA Editions, 1997, 77 (3), pp.399-409
Le Lait, INRA Editions, 1997, 77 (3), pp.399-409
Summary - Bovine whey proteins such as œ-lactalbumin and ~-Iactoglobulin are with bovine caseins the most commonly used proteins in infant formulas owing to their high nutritional value. However, these cow milk components are not always weil tolerat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d0de034df5261569199c566088bf9a9
https://hal.archives-ouvertes.fr/hal-00929534/document
https://hal.archives-ouvertes.fr/hal-00929534/document
Publikováno v:
Pancreas
Pancreas, Lippincott, Williams & Wilkins, 1997, 15 (3), pp.258-264
HAL
Pancreas, Lippincott, Williams & Wilkins, 1997, 15 (3), pp.258-64
Pancreas, Lippincott, Williams & Wilkins, 1997, 15 (3), pp.258-264
HAL
Pancreas, Lippincott, Williams & Wilkins, 1997, 15 (3), pp.258-64
International audience; The specific regulation of pancreatic elastase I and II mRNA expression as well as of the protein, RNA, and DNA contents were determined during ontogeny in the calf. Specific activities and mRNA concentrations were quantified
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::656ff8878034bd83750641a628ffd6ca
https://hal.inrae.fr/hal-02695291
https://hal.inrae.fr/hal-02695291
Autor:
Wojciech Ardelt
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure. 393:267-273
Some molecular properties of the elastase II preparation, homogenous in ultracentrifugation, have been determined. The molecular weight is 25 000, the sedimentation coefficient and the diffusion coefficient are 3.69·10−13 s−1 and 12.09·10−7 c