Conjugation of biogenic and synthetic polyamines with trypsin and trypsin inhibitor

RSC Advances ◽  
2016 ◽  
Vol 6 (59) ◽  
pp. 53690-53697 ◽  
Author(s):  
P. Chanphai ◽  
T. J. Thomas ◽  
H. A. Tajmir-Riahi
Keyword(s):  
Trypsin Inhibitor ◽  
Polyamine Analogues ◽  
Protein Conjugates ◽  
Synthetic Polyamines

Polyamine–protein conjugates can be used as delivery tools to transport antitumor polyamine analogues.

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

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.

Cardiological Biopharmaceuticals in the Conception of Drug Targeting Delivery: Practical Results and Research Perspectives

Acta Naturae ◽  
2012 ◽  
Vol 4 (3) ◽  
pp. 72-81 ◽  
Author(s):  
A. V. Maksimenko
Keyword(s):  
Cell Adhesion Molecules ◽  
Drug Targeting ◽  
Interventional Procedures ◽  
Target Localization ◽  
Clinical Use ◽  
Protein Conjugates ◽  
Research Perspectives ◽  
Significant Interest ◽  
Targeting Delivery ◽  
Molecular Sizes

The results of the clinical use of thrombolytic and antithrombotic preparations developed on the basis of protein conjugates obtained within the framework of the conception of drug targeting delivery in the organism are considered. A decrease has been noted in the number of biomedical projects focused on these derivatives as a result of various factors: the significant depletion of financial and organizational funds, the saturation of the pharmaceutical market with preparations of this kind, and the appearance of original means for interventional procedures. Factors that actively facilitate the conspicuous potentiation of the efficacy of bioconjugates were revealed: the biomedical testing of protein domains and their selected combinations, the optimization of molecular sizes for the bioconjugates obtained, the density of target localization, the application of cell adhesion molecules as targets, and the application of connected enzyme activities. Enzyme antioxidants and the opportunity for further elaboration of the drug delivery conception via the elucidation and formation of therapeutic targets for effective drug reactions by means of pharmacological pre- and postconditioning of myocardium arouse significant interest.

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

PRODUCTION AND CHARACTERIZATION OF ANTIBODIES ELICITED BY DIFFERENT ALDOSTERONE-PROTEIN CONJUGATES

1972 ◽  
Vol 68 (3_Suppl) ◽  
pp. S32
Author(s):  
W. Vetter ◽  
E. Freedlender ◽  
E. Haber
Keyword(s):  
Protein Conjugates
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