Dermasterias imbricata trypsin 1: an enzyme which rapidly hydrolyzes the reactive-site peptide bonds of protein trypsin inhibitors

Biochemistry ◽  
1980 ◽  
Vol 19 (1) ◽  
pp. 124-131 ◽  
Author(s):  
David A. Estell ◽  
Michael Laskowski
Keyword(s):  
Trypsin Inhibitors ◽  
Reactive Site ◽  
Peptide Bonds

scholarly journals Trypsin inhibitors in turnip (Brassica rapa L.) seeds

2014 ◽  
Vol 58 (4) ◽  
pp. 563-573 ◽  
Author(s):  
Anna Wilimowska-Pelc
Keyword(s):  
Molecular Weight ◽  
Peptide Bond ◽  
Ion Exchange Chromatography ◽  
Trypsin Inhibitors ◽  
Exchange Chromatography ◽  
Trypsin Activity ◽  
Reactive Site ◽  
Salting Out ◽  
Similar Molecular Weight ◽  
Immobilized Trypsin

A method of trypsin inhibitors isolation from turnip seeds is described. Inhibitors were extracted with 0.01 N HCI, concentrated by salting out with ammonium sulfate, and purified using ion-exchange chromatography on Sp-Sephadex C-25, QAE-Sephadex A-25 and affinity chromatography on immobilized trypsin. Among the three isolated inhibitors, ITR I of molecular weight 15.9 kDa, pl. 6,4, inhibited trypsin activity only. Inhibitors ITR II and ITR Ill inhibited also chymotrypsin activity, they had similar molecular weight (about 10 kDa), but their pI is 7.5 and over 10, respectively. Arginine residue occurred in P, position of the reactive site of inhibitors ITR I and ITR III, while in ITR 11 this position was occupied by lysine residue. Electrophoresis on polyacrylamide gel revealed that each inhibitor possessed two protein fractions, probably a virgin and modified form, with the reactive site peptide bond broken by trypsin.

scholarly journals The Reactive Site of Trypsin Inhibitors

1966 ◽  
Vol 241 (17) ◽  
pp. 3955-3961 ◽  
Author(s):  
Kyoichi Ozawa ◽  
Michael Laskowski
Keyword(s):  
Trypsin Inhibitors ◽  
Reactive Site

Solvent-assisted osmium staining of butyl acrylate and ethylene-propylene-diene in a styrene acrylonitrile matrix

1993 ◽  
Vol 51 ◽  
pp. 900-901 ◽  
Author(s):  
Gudrun A. Hutchins
Keyword(s):  
Butyl Acrylate ◽  
Room Temperature ◽  
Osmium Tetroxide ◽  
Staining Procedure ◽  
Reactive Site ◽  
Ethylene Propylene ◽  
Minimal Distortion ◽  
Styrene Acrylonitrile ◽  
Engineering Polymers ◽  
Effective Reaction

In order to optimize the toughening effect of elastomers in engineering polymers, it is necessary to characterize the size, morphology and dispersion of the specific elastomer within the polymer matrix. For unsaturated elastomers such as butadiene or isoprene, staining with osmium tetroxide is a well established procedure. The residual carbon-carbon double bond in these materials is the reactive site and forms a 1,2-dilato complex with the OsO4. Incorporation of osmium tetroxide into the elastomer not only produces sufficient contrast for TEM, but also crosslinks the elastomer sufficiently so that ultramicrotomy can be accomplished at room temperature with minimal distortion.Blends containing saturated elastomers such as butyl acrylate (BA) and ethylene propylene diene monomer (EPDM) cannot be stained directly with OsO4 because effective reaction sites such as C=C or -NH2 are not available in sufficient number. If additional reaction sites can be introduced selectively into the elastomer by a chemical reaction or the absorption of a solvent, a modified, two-step osmium staining procedure is possible.

Alpha-Amylase/Trypsin Inhibitors, novel activators of innate immunity in ex-vivo tissue explants

2013 ◽  
Vol 51 (08) ◽  
Author(s):  
V Zevallos ◽  
P Olinga ◽  
Y Junker ◽  
PB Tung ◽  
N Volz ◽  
...  
Keyword(s):  
Innate Immunity ◽  
Ex Vivo ◽  
Trypsin Inhibitors ◽  
Alpha Amylase ◽  
Tissue Explants ◽  
Ex Vivo Tissue

Synthesis of cyclic citrullinated peptides targeting rheumatoid arthritis autoantibodies based on sunflower trypsin inhibitors

Planta Medica ◽  
2016 ◽  
Vol 81 (S 01) ◽  
pp. S1-S381
Author(s):  
C Eriksson ◽  
S Gunasekera ◽  
C Cerqueira ◽  
PJ Jacobsson ◽  
U Göransson
Keyword(s):  
Rheumatoid Arthritis ◽  
Trypsin Inhibitors

Studies on the Degradation of Human Fibrinogen by Plasmin and Trypsin

1966 ◽  
Vol 16 (03/04) ◽  
pp. 526-540 ◽  
Author(s):  
E. A Beck ◽  
D. P Jackson
Keyword(s):  
Physicochemical Properties ◽  
Electrophoretic Mobility ◽  
Rapid Loss ◽  
Clotting System ◽  
Human Fibrinogen ◽  
Peptide Bonds ◽  
Physico Chemical ◽  
Starch Gel ◽  
Ph Stat ◽  
Rapid Appearance

SummaryThe effects of trypsin and plasmin on the functional and physicochemical properties of purified human fibrinogen were observed at various stages of proteolysis. Concentrations of plasmin and trypsin that produced fibrinogenolysis at comparable rates as measured in a pH stat produced, at similar rates, loss of precipitability of fibrinogen by heat and ammonium sulphate and alterations in electrophoretic mobility on starch gel. Trypsin produced a more rapid loss of clottability of fibrinogen and a more rapid appearance of inhibitors of the thrombin-fibrinogen clotting system than did plasmin. Consistent differences were noted between the effects of trypsin and plasmin on the immunoelectrophoretic properties of fibrinogen during the early stages of proteolysis.These results are consistent with the hypothesis that trypsin initially reacts with the same peptide bonds of fibrinogen that are split by thrombin, but these same bonds do not appear to be split initially by plasmin. Measurement of the various functional and physico-chemical changes produced by the action of trypsin and plasmin on fibrinogen can be used to recognize various stages of proteolysis.

Sign in / Sign up

Export Citation Format

Share Document