Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Rui Qing Qian"'
Autor:
Siebold, Bernhard1, Rui-Qing Qian1, Glanville, Robert W.1, Hofmann, Hans1, Deutzmann, Rainer1, Kühn, Klaus1
Publikováno v:
European Journal of Biochemistry. 11/2/87, Vol. 168 Issue 3, p569-575. 7p.
Autor:
Elaine Schwartz, Rui-Qing Qian, Julia M. Ross, Joel L. Moake, Huey-Ju Kuo, Jacob H. Rand, Robert W. Glanville, Larry V. McIntire
Publikováno v:
Thrombosis and Haemostasis. 79:155-161
SummaryThe vascular subendothelium contains macromolecular structures called microfibrils. Type VI collagen is one protein found in microfibrils that supports platelet adhesion and aggregation and we have previously evaluated the roles of platelet re
Publikováno v:
Journal of Biological Chemistry. 269:26630-26634
The extracellular matrix protein fibrillin-1 is a major component of elastic microfibrils, which are complex assemblies of several proteins and are found in most connective tissues, frequently associated with elastin. Fibrillin-1 contains 43 precurso
Publikováno v:
FEBS Letters. 297:143-146
The stoichiometric complex formed between porcine β-trypsin and the Momordica charantia , Linn. Cucurbitaceae trypsin inhibitor-A (MCTI-A) was crystallized and its X-ray crystal structure determined using molecular replacement method. The primary se
Publikováno v:
Chinese Journal of Chemistry; Nov1999, Vol. 17 Issue 6, p658-673, 16p
Autor:
Klaus Kähn, Hans Hofmann, Robert W. Glanville, Rui-Qing Qian, Bernhard Siebold, Rainer Deutzmann
Publikováno v:
European Journal of Biochemistry. 168:569-575
The amino acid sequence of the 212-residues-long N-terminal aggregation and cross-linking region of the alpha 2(IV) chain of human basement membrane collagen is presented. Comparing this with the primary structure of alpha 1(IV)7S [Glanville et al. (
Publikováno v:
FEBS Letters. 234:35-38
A trypsin inhibitor (MCI-3) was isolated from the seeds of Momordica charantia Linn. Cucurbitaceae in three steps involving the affinity chromatography, CM-Sephadex chromatography and HPLC. It is composed of 62 amino acid residues: Asp3Thr.5Ser4Glu5P
Autor:
Hans Dieringer, Yoshihiko Yamada, Klaus Kühn, Ilse Oberbäumer, Robert W. Glanville, Wilfried Babel, Rui-Qing Qian, Bernhard Siebold, Tilman Voss, Ulla Schwarz
Publikováno v:
Annals of the New York Academy of Sciences. 460
Publikováno v:
European journal of biochemistry. 152(1)
The amino acid sequence of the 216-residue-long N-terminal aggregation and cross-linking 7S domain of the alpha 1 (IV) chain of human placental basement membrane collagen is presented. The N terminus of the alpha 1 (IV) chain starts with a non-triple