Transcriptome Analysis of the Duodenum, Pancreas, Liver, and Muscle from Diabetic Goto-Kakizaki Rats Fed a Trypsin Inhibitor Derived from Squid Viscera

2012 ◽  
Vol 60 (22) ◽  
pp. 5540-5546 ◽  
Author(s):  
Kohsuke Adachi ◽  
Kana Fukumorita ◽  
Michihiro Araki ◽  
Nobuhiro Zaima ◽  
Zhi-Hong Yang ◽  
...  
Keyword(s):  
Trypsin Inhibitor ◽  
Transcriptome Analysis ◽  
Squid Viscera

Transcriptome Analysis of the Duodenum in Wistar Rats Fed a Trypsin Inhibitor Derived from Squid Viscera

2011 ◽  
Vol 59 (16) ◽  
pp. 9001-9010 ◽  
Author(s):  
Kohsuke Adachi ◽  
Kana Fukumorita ◽  
Michihiro Araki ◽  
Nobuhiro Zaima ◽  
Satoru Chiba ◽  
...  
Keyword(s):  
Trypsin Inhibitor ◽  
Transcriptome Analysis ◽  
Wistar Rats ◽  
Squid Viscera

Transcriptome analysis of pediatric cALL versus normal tissue reveals a novel signature of the malignant phenotype

2009 ◽  
Vol 221 (03) ◽  
Author(s):  
GHS Richter ◽  
UE Hattenhorst ◽  
B Beinvogl ◽  
D Schenk ◽  
MS Staege ◽  
...  
Keyword(s):  
Transcriptome Analysis ◽  
Normal Tissue ◽  
Malignant Phenotype

The role of the N34S mutation in the trypsin inhibitor gene SPINK1 in patients with chronic pancreatitis from Romania

2009 ◽  
Vol 47 (06) ◽  
Author(s):  
B Diaconu ◽  
A Schneider ◽  
R Pfützer ◽  
T Mocan ◽  
M Scăfaru ◽  
...  
Keyword(s):  
Chronic Pancreatitis ◽  
Trypsin Inhibitor ◽  
N34s Mutation ◽  
Inhibitor Gene

Transcriptome analysis in HepG2 cells revealed multiple activity mechanisms of a Tibetan polyherbal formula

2012 ◽  
Vol 33 (S 01) ◽  
Author(s):  
K Becker ◽  
A Klein ◽  
OA Wrulich ◽  
P Gruber ◽  
D Fuchs ◽  
...  
Keyword(s):  
Transcriptome Analysis ◽  
Hepg2 Cells

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.

Factor X Activation by washed human platelets

1979 ◽  
Author(s):  
E van Wijk ◽  
L Kahlé ◽  
J ten Cate
Keyword(s):  
Human Factors ◽  
Trypsin Inhibitor ◽  
Calcium Ions ◽  
Factor Xa ◽  
Human Platelets ◽  
Soybean Trypsin Inhibitor ◽  
Thrombin Inhibitor ◽  
Chromogenic Substrate ◽  
Factor X ◽  
Factor X Activation

In a system of washed human platelets, Ca2+and purified human factors X anc II, a sufficient amount of thrombin is generated in about 10 minutes to aggregate the platelets. This thrombin is formed through the activation of FX by the platelets. In a system with either FX or FII present, no aggregation occurs. In addition no aggregation is observed when hirudin, a specific thrombin inhibitor, or when soybean trypsin inhibitor, which inhibits factor Xa, are added to the mixture. The formation of factor Xa can be monitored indirectly through the generation of thrombin, in the presence of an excess of prothrombin, using a thrombin sensitive chromogenic substrate. When washed platelets are incubated with FX alone for 10 minutes, no aggregation occurs and after the addition of prothrombin aggregation starts within 6 minutes. These findings confirm that washed platelets possess a factor X activating property. The generation of FXa proceeds in the absence of added Ca2+, whereas in the presence of Ca2+factor Xa activity reaches a maximum in 3 minutes, whereafter the activity progressively decreases. This may be due to the binding of Xa to the platelets in the presence of calcium ions.

THE EXCRETION OF TRYPSIN INHIBITOR IN URINE IN NORMAL PERSONS

1959 ◽  
Vol 30 (2) ◽  
pp. 285-295 ◽  
Author(s):  
Hans J. Faarvang
Keyword(s):  
Trypsin Inhibitor

Deregulation of Sertoli and Leydig cells function in patients with Klinefelter syndrome as evidenced by testis transcriptome analysis

2015 ◽  
Author(s):  
Alberto Ferlin ◽  
Marco D'Aurora ◽  
Marta Di Nicola ◽  
Andrea Garolla ◽  
Luca De Toni ◽  
...  
Keyword(s):  
Transcriptome Analysis ◽  
Leydig Cells ◽  
Klinefelter Syndrome
Sign in / Sign up

Export Citation Format

Share Document