THE DISTRIBUTION OF TRYPSIN AND CHYMOTRYPSIN INHIBITORS IN POTATO TUBERS

Potato peel contains trypsin and chymotrypsin inhibitors at levels similar to those in other parts of the tuber. The levels of these inhibitors differ among potato cultivars (P < 0.01). The proteolytic enzyme inhibitors may have to be deactiviated before peel waste can be efficiently utilized by pigs. Key words: Potato steam peel, trypsin, chymotrypsin, proteolytic enzyme inhibitor

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Preparation and Properties of Human Prothrombin Complex

Thrombosis and Haemostasis ◽

10.1055/s-0038-1654240 ◽

1970 ◽

Vol 24 (03/04) ◽

pp. 325-333 ◽

Cited By ~ 4

Author(s):

G. H Tishkoff ◽

L. C Williams ◽

D. M Brown

Keyword(s):

Molecular Weight ◽

Proteolytic Enzyme ◽

Enzyme Inhibitor ◽

Specific Activity ◽

Crystalline Form ◽

Sedimentation Equilibrium ◽

Crystalline Complex ◽

Interaction Product ◽

Proteolytic Enzyme Inhibitor ◽

Purification Scheme

SummaryAs a corollary to our previous studies with bovine prothrombin, we have initiated a study of human prothrombin complex. This product has been isolated in crystalline form as a barium glycoprotein interaction product. Product yields were reduced compared to bovine product due to the increased solubility of the barium glycoprotein interaction product. On occasion the crystalline complex exhibited good yields. The specific activity of the crystalline complex was 1851 Iowa u/mg. Further purification of human prothrombin complex was made by removal of barium and by chromatography on Sephadex G-100 gels. The final product evidenced multiple procoagulant activities (II, VII, IX and X). The monomeric molecular weight determined by sedimentation equilibrium in a solvent of 6 M guanidine-HCl and 0.5% mercaptoethanol was 70,191 ± 3,057 and was homogeneous with respect to molecular weight. This product was characterized in regard to physical constants and chemical composition. In general, the molecular properties of human prothrombin complex are very similar to the comparable bovine product. In some preparations a reversible proteolytic enzyme inhibitor (p-aminophenylarsonic acid) was employed in the ultrafiltration step of the purification scheme to inhibit protein degradation.

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IMPROVEMENT OF THE SEPTIC LUNG LESION BY TREATMENT WITH A PROTEOLYTIC ENZYME INHIBITOR

Anesthesiology ◽

10.1097/00000542-198209001-00132 ◽

1982 ◽

Vol 57 (3) ◽

pp. A132-A132

Author(s):

D. L. Traber ◽

L. Sziebert ◽

T. Adams ◽

N. Henriksen ◽

L. D. Traber

Keyword(s):

Proteolytic Enzyme ◽

Enzyme Inhibitor ◽

Lung Lesion ◽

Proteolytic Enzyme Inhibitor

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Effect of various drugs on the binding of thyrotrophin to thyroid plasma membranes

Acta Endocrinologica ◽

10.1530/acta.0.1000519 ◽

1982 ◽

Vol 100 (4) ◽

pp. 519-526

Author(s):

Yasuto Baba ◽

Yoshinobu Nakao ◽

Michizo Kishihara ◽

Nobuhisa Kobayashi ◽

Hiroyuki Kimoto ◽

...

Keyword(s):

Plasma Membranes ◽

Enzyme Inhibitors ◽

Enzyme Inhibitor ◽

Human Thyroid ◽

Dependent Manner ◽

Protective Effects ◽

Proteolytic Enzyme Inhibitor ◽

Erythrocyte Lysis ◽

Adrenergic Blocking ◽

Dose Dependent

Abstract. Effects of enzyme inhibitors and membraneactive drugs on the binding of 125I-labelled thyroidstimulating hormone (TSH) to human thyroid membranes and membrane adenylate cyclase (AC) activity were studied. FOY®, a synthetic polyvalent proteolytic enzyme inhibitor, Trasylol®, α- and β-adrenergic blocking agents, tranquilizers, anti-histamines and polyene antibiotics enchanced TSH binding in a dose-dependent manner, whereas selective enzyme inhibitors and adrenergic stimulating agents had no effect. Both propranolol and FOY inhibited basal and TSH stimulated AC activity of thyroid membranes. FOY, as well as propranolol was found to have protective effects on hypotonic erythrocyte lysis. These results suggest that propranolol and FOY increased TSH binding by the same mechanism, probably the so-called membrane-stabilizing effects. Although the detailed mechanisms underlying the increased TSH binding by these drugs remain unknown, they may change the membrane structure, thereby enhancing the TSH receptor affinity.

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THE USE OF PROTEOLYTIC ENZYME INHIBITOR (TRASYLOL) IN RADIORECEPTOR ASSAY OF TSH - ITS APPLICATION TO MEASURING THYROID STIMULATING IMMUNOGLOBULINS (TSI) IN THYROID DISEASES

Acta Endocrinologica ◽

10.1530/acta.0.0880065 ◽

1978 ◽

Vol 88 (1) ◽

pp. 65-74 ◽

Cited By ~ 4

Author(s):

Michizo Kishihara ◽

Yoshinobu Nakao ◽

Yasuto Baba ◽

Shozo Ohgo ◽

Shigeru Matsukura ◽

...

Keyword(s):

Proteolytic Enzyme ◽

Enzyme Inhibitor ◽

Great Majority ◽

Thyroid Stimulating Hormone ◽

Radioreceptor Assay ◽

Human Thyroid ◽

Graves Disease ◽

Stable Method ◽

Thyroid Stimulating Immunoglobulins ◽

Proteolytic Enzyme Inhibitor

ABSTRACT In order to estimate thyroid stimulating immunoglobulins (TSI) in serum, a stable, reproducible and sensitive radioreceptor assay (RRA) capable of detecting 100 μU of thyroid stimulating hormone (TSH) has been developed using a proteolytic enzyme inhibitor (Trasylol), partially purified human TSH and particulate fractions of human thyroid homogenate. The binding of 125I-labelled TSH to the crude thyroid membranes was significantly increased from 2–3 % to 15–20 % in the presence of Trasylol (2000 KIU per tube). Further investigations suggested that Trasylol might inhibit the aggregation of 125I-labelled TSH during incubation with these membranes. With this assay system, the serum immunoglobulins from a great majority of untreated patients with Graves' disease were shown to inhibit the binding of 125I-labelled TSH to those membranes more markedly than those from control subjects. Therefore, this RRA for TSH was considered to provide a sensitive and stable method for detecting TSI.

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Action of a Proteolytic Enzyme Inhibitor on Blood Coagulation in Vitro

Thrombosis and Haemostasis ◽

10.1055/s-0038-1655028 ◽

1967 ◽

Vol 18 (01/02) ◽

pp. 190-197 ◽

Cited By ~ 2

Author(s):

B Blombäck ◽

Margareta Blombäck ◽

P Olsson

Keyword(s):

Blood Coagulation ◽

Proteolytic Enzyme ◽

Enzyme Inhibitor ◽

Factor V ◽

Generation System ◽

Antifibrinolytic Agents ◽

Coagulation Activity ◽

Serum Factors ◽

Proteolytic Enzyme Inhibitor

SummaryThe action of the kallikrein and trypsin inhibitor, Trasylol, has been studied in a three-stage thrombin generation system. It has been found that Trasylol inhibits one or several of the early reactions of blood coagulation. The inhibition of the early stages is dependent on the concentration of inhibitor, serum factors and factor VIII. The activation of factor V by tiger snake venom is not inhibited by Trasylol. The inhibition is most probably on one or several of the reactions preceding the factor V involved step.Some other known antifibrinolytic agents have also been tested for anti-coagulation activity.

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