scholarly journals Effect of Urinary Trypsin Inhibitor on Preterm Labor with High Granulocyte Elastase Concentration in Cervical Secretions

2010 ◽  
Vol 77 (2) ◽  
pp. 80-85 ◽  
Author(s):  
Masako Hayashi ◽  
Atsuko Oya ◽  
Hidehiko Miyake ◽  
Akihito Nakai ◽  
Toshiyuki Takeshita
Keyword(s):  
Trypsin Inhibitor ◽  
Preterm Labor ◽  
Urinary Trypsin Inhibitor ◽  
Granulocyte Elastase

Urinary trypsin inhibitor: a new drug to treat preterm labor: a comparative study with ritodrine

1996 ◽  
Vol 67 (2) ◽  
pp. 133-138 ◽  
Author(s):  
Naohiro Kanayama ◽  
Emad El Maradny ◽  
Nobuhiro Yamamoto ◽  
Naoki Tokunaga ◽  
Kayoko Maehara ◽  
...  
Keyword(s):  
Comparative Study ◽  
Trypsin Inhibitor ◽  
Preterm Labor ◽  
Urinary Trypsin Inhibitor ◽  
New Drug

Human Granulocyte Elastase is Inhibited by the Urinary Trypsin Inhibitor

1982 ◽  
Vol 363 (2) ◽  
pp. 1167-1176 ◽  
Author(s):  
Brittt-Marie JÖNSSON ◽  
Christel LÖFFLER ◽  
Kjell OHLSSON
Keyword(s):  
Trypsin Inhibitor ◽  
Urinary Trypsin Inhibitor ◽  
Granulocyte Elastase

URINARY TRYPSIN INHIBITOR AND GRANULOCYTE ELASTASE IN BALF -THE DIFFERENCE WITH AGE

1998 ◽  
Vol 86 (Supplement) ◽  
pp. 133S
Author(s):  
J. Kawasaki ◽  
A. Katayama ◽  
Y. Okamoto ◽  
I. Ishizuka ◽  
T. Kawazoe ◽  
...  
Keyword(s):  
Trypsin Inhibitor ◽  
Urinary Trypsin Inhibitor ◽  
Granulocyte Elastase ◽  
The Difference

Low Molecular Weight Trypsin-Plasmin Inhibitors Isolated from Papain Treated Urinary Trypsin Inhibitor

1982 ◽  
Vol 47 (01) ◽  
pp. 014-018 ◽  
Author(s):  
H Sumi ◽  
N Toki ◽  
S Takasugi ◽  
S Maehara ◽  
M Maruyama ◽  
...  
Keyword(s):  
Trypsin Inhibitor ◽  
Gel Electrophoresis ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Chromatography ◽  
Urinary Trypsin Inhibitor ◽  
Plasmin Activity ◽  
Molecular Weights ◽  
Plasmin Inhibitors

SummaryPapain treatment of human urinary trypsin inhibitor (UTI67; mol. wt. 43,000 by SDS-polyacrylamide gel electrophoresis, specific activity 1,897 U/mg protein) produced four new protease inhibitors, which were highly purified by gel chromatography on Sephadex G-100 and isoelectric focusing. The purified inhibitors (UTI26, UTI9-I, UTI9-II, and UTI9-III) were shown to be homogeneous by polyacrylamide disc gel electrophoresis, and had apparent molecular weights of 26,000, 9,000, 9,000, and 9,800, respectively, by sodium dodecyl sulfate gel electrophoresis. During enzymatic degradation of UTI67, the amino acid compositions changed to more basic, and the isoelectric point increased from pH 2.0 (UTI67) to pHs 4.4, 5.2, 6.6, and 8.3 (UTI26, UTI9-I, UTI9-II, and UTI9-III), respectively. Both the parent and degraded inhibitors had anti-plasmin activity as well as antitrypsin and anti-chymotrypsin activities. Much higher anti-plasmin/anti-trypsin and anti-plasmin/anti-chymotrypsin activities were observed in the degraded inhibitors than in the parent UTI67. They competitively inhibited human plasmin with Ki values of 1.13 X 10-7 - 2.12 X 10-6 M (H-D-Val-Leu-Lys-pNA substrate). The reactions were very fast and the active site of the inhibitors to plasmin was thought to be different from that to trypsin or chymotrypsin.

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