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Use of crystalline soybean trypsin inhibitor in acute hemorrhagic pancreatitis in dogs.

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Hemorrhagic principles in the venom of Bitis arietans, a viperous snake. II. Enzymatic properties with special reference to substrate specificity.

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The optimal pH of the proteinase activity of hemorrhagins, BHRa and BHRb, isolated from the venom of Bitis arietans (puff adder) is pH 9. The activity was inhibited by metal chelating agents such as EDTA, 1,10-phenanthroline and 8-hydroxyquinoline, but not by phenylmethanesulfonyl fluoride and

Isolation and characterization of hemorrhagic factors a and b from the venom of the Chinese habu snake (Trimeresurus mucrosquamatus).

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Hemorrhagic factors a and b were isolated from Trimeresurus mucrosquamatus venom by Sephadex G-100, CM-Sephadex C-50 and DEAE-Sephacel column chromatographies. The hemorrhagic factors were homogeneous, as established by a single band on acrylamide gel electrophoresis, isoelectric focusing and sodium

Purification and characterization of the hemorrhagic factor II from the venom of the Bushmaster snake (Lachesis muta muta).

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Hemorrhagic factor II (LHF-II) was isolated from Lachesis muta muta (Bushmaster snake) venom using column chromatographies on Sephadex G-100, CM-Sepharose CL-6B and two cycles on Sephadex G-50. This preparation was devoid of phospholipase A2 as well as of the enzymes active on arginine synthetic

Hemorrhagic principles in the venom of Bitis arietans, a viperous snake. I. Purification and characterization.

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Two hemorrhagic principles (Bitis arietans hemorrhagin a and b: abbreviated as BHRa and BHRb) were purified from the venom of the viperous snake Bitis arietans (puff adder) by gel filtration, ion-exchange and absorption chromatography. A 10-fold purification was achieved for BHRa and 7-fold for BHRb

Characterization of hemorrhagic principles from Trimeresurus gramineus snake venom.

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In addition to alpha-fibrinogenase (hemorrhagin I, HR1), a potent hemorrhagic principle (hemorrhagin II, HR2) was purified from Trimeresurus gramineus venom. It was homogeneous as judged by SDS-polyacrylamide gel electrophoresis. HR2 was a single peptide chain containing 10% carbohydrate with a

Hemorrhagic toxin from the venom of Agkistrodon bilineatus (common cantil).

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1. Hemorrhagic toxin was isolated from Agkistrodon bilineatus (Common cantil) venom using a three-step purification procedure to obtain 32.8 mg of purified hemorrhagic toxin from 700 mg of crude venom. 2. The purified toxin was homogeneous by disc polyacrylamide gel electrophoresis at pH 8.3, and by

Hemorrhagic protease from the venom of Calloselasma rhodostoma.

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1. A hemorrhagic protease I (HP-I) was isolated from Calloselasma rhodostoma venom by Sephadex G-75, DEAE-Sephacel and Q-Sepharose column chromatographies. 2. Homogeneity was established by the formation of a single band in acrylamide gel electrophoresis. 3. HP-I has a molecular weight of 34,800 and

Isolation and characterization of hemorrhagic toxin g from the venom of Crotalus atrox (western diamondback rattlesnake).

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Hemorrhagic toxin g (HT-g) was isolated from Crotalus atrox (western diamondback rattlesnake) venom using a five-step purification procedure to obtain approximately equal to 5.9 mg of purified HT-g from 2.0 g of crude venom. The purified toxin was homogeneous by disc electrophoresis on

Purification and characterization of BaH4, a hemorrhagic metalloproteinase from the venom of the snake Bothrops asper.

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A hemorrhagic metalloproteinase, named BaH4, was isolated from the venom of the snake Bothrops asper by a combination of ion-exchange chromatography on DEAE-Sepharose and gel filtration on Sephacryl S-200. BaH4 is a 69 kDa protein with a pI of 5.3. It was recognized by antibodies raised against

Isolation and characterization of a metalloproteinase with weak hemorrhagic activity from the venom of the snake Bothrops asper (terciopelo).

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A metalloproteinase, named BaP1, was purified to homogeneity from the venom of Bothrops asper (Pacific region) of Costa Rica by ion-exchange chromatography on CM-Sephadex and gel filtration on Sephacryl S-200. The enzyme has a mol. wt of 24,000 and contains few Cys and high numbers of Asp, Leu, Ser

Selective kallikrein inhibitors alter human neutrophil elastase release during extracorporeal circulation.

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Cardiopulmonary bypass causes hemorrhagic complications and initiates a biochemical and cellular "whole body inflammatory response." This study investigates whether a variety of selective inhibitors of the contact pathway of intrinsic coagulation modulate complement and neutrophil activation during

Some effects of proteolytic inhibitors on tissue injury and systemic anaphylaxis.

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A study was made of the development of various forms of local and systemic injury in animals treated with inhibitors of proteolytic activity. The agents used were tosylarginine methyl ester (TAME), epsilon aminocaproic acid (EACA), and soybean trypsin inhibitor (SBTI). 1. Hemorrhagic necrosis in the

Purification and partial characterization of a chymotrypsin-like serine fibrinolytic enzyme from Bacillus amyloliquefaciens FCF-11 using corn husk as a novel substrate.

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A non-toxic, direct-acting fibrinolytic enzyme, FCF-11, from a newly isolated Bacillus amyloliquefaciens FCF-11 was purified, characterized and assayed both in vitro and in vivo for its thrombolytic potential. Corn husk was used as for the first time as the sole carbon/nitrogen source for enzyme

Amidolytic assay of factor XI in human plasma--significance of kallikrein for the activity measured.

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Factor XI (FXI) deficiency is associated with an abnormal bleeding state. The extent of bleeding does not correlate well with the plasma concentration of FXI, and it has been suggested that also unknown factors interfere with the bleeding tendency. In a recent paper (Thromb. Res. 74, 477-485, 1994)

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