Studies on the Effect of Plasminogen Activator on the Interaction between α2-Macroglobulin and Plasmin

Toki, Naotika; Sumiyoshi, Tetsuya; Sumi, Hiroyuki; Yamura, T

doi:10.1055/s-0038-1648671

Cited by 9 publications

(4 citation statements)

References 8 publications

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“…Glu-plg and plasmin were prepared according to the method described in previous reports (10,11). The specific abtivity of purified plasmin was 15.3 casein units/mg protein.…”

Section: Preparation Of Glu-plg and Plasminmentioning

confidence: 99%

Studies on the Activation Mechanism of Fibrinolytic Enzyme System in Plasma by Human Pancreatic Elastase

et al. 1982

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SummaryIn the present study, the activation mechanism of fibrinolytic enzyme system in plasma by human pancreatic elastase was investigated. It was confirmed that human pancreatic elastase not only converted the co-existing plasminogen to low molecular weight-plasminogen which could be easily activated by the activator, but also inhibited α2-macroglobulin and α2-plasmin inhibitor which are antiactivators or fast reacting antiplasmins, and consequently, induced the activation of the fibrinolytic enzyme system in plasma.

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“…Glu-plg and plasmin were prepared according to the method described in previous reports (10,11). The specific abtivity of purified plasmin was 15.3 casein units/mg protein.…”

Section: Preparation Of Glu-plg and Plasminmentioning

confidence: 99%

Studies on the Activation Mechanism of Fibrinolytic Enzyme System in Plasma by Human Pancreatic Elastase

et al. 1982

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“…The caseinolytic activity was measured by the method described in a previous report [7]. The final concentration of casein was 2%.…”

Section: Enzyme and Protein Assaymentioning

confidence: 99%

A Case of Ruptured Hepatoma Followed by Elastase-Induced Disseminated Intravascular Coagulation

Sumiyoshi¹,

Nishiki²,

Kanao³

et al. 1985

Enzyme

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In the present study, the first case of ruptured hepatoma followed by disseminated intravascular coagulation is reported. An elastase-like enzyme which possessed elastolytic and caseinolytic activities was confirmed from patient plasma. On the other hand, no elastase activity was detected in the plasma of patients with hepatitis, liver cirrhosis or hepatoma without disseminated intravascular coagulation. The patient plasma did not possess H-D-Val-Leu-Lys-p-nitroanilide hydrochloride, succinyl-L-alanyl-L-alanyl-p-nitroanilide, and pyro-Glu-Pro-Val-p-nitroanilide amidolytic activities. However, when chromatographed on Sephadex G-200, the presence of low-molecular weight plasminogen was confirmed. Its molecular weight was approximately 52,000. A slight decrease of α2-plasmin inhibitor was noted, but no decrease of α2-macroglobulin was detected.

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“…Human plasma a2-macroglobulin (a2-M), arantitrypsin (aiAt) and Cl-inhibitor (Cl-Inh) were purified by the method described in previous reports [19][20][21], The IaTI was prepared according to the method of Steinbuch [22], The concentration of protein in a2-M, ai-At precipitin line with human plasma euglobulin fraction or purified IaTI, but did not react with purified a2-M, arAt or Cl-Inh. When anti-UTI-III antiserum was diffused instead of anti-UTI-I antiserum, the result was the same as in figure 2.…”

Section: Preparation Of Proteinase Inhibitors In Human Serummentioning

confidence: 99%

Immunochemical Studies of Human Urinary Trypsin Inhibitor

Maehara¹,

Sumi²,

Toki³

1981

Enzyme

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Antisera against purified urinary trypsin inhibitor (UTI-I, molecular weight 67,000) and UTI-III (molecular weight 23,000) were first produced in rabbits. Both anti- UTI-I and anti-UTI-III sera formed a single immunoprecipitin line with human plasma intera- trypsin inhibitor (IaTI), whereas two immunoprecipitin lines were formed with crude urine. It was speculated that both UTI-I and UTI-III might be present in normal human urine. In the present study, the inhibitory effects of anti-UTI sera on UTI activity were examined by three different assay methods. The results indicated that the inhibitory effect was almost immediate. Although the inhibitory effect of anti-UTI-III serum on UTI-III was almost of the same degree of completeness for the three assay methods, UTI-I was partially inhibited by the anti-UTI-I serum when residual trypsin activity was measured by the caseinolytic or fibrinolytic assay method. This discrepancy was considered to be due to the difference in conformational change between UTI-I and UTI-III by antigen-antibody reaction.

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Studies on the Effect of Plasminogen Activator on the Interaction between α2-Macroglobulin and Plasmin

Cited by 9 publications

References 8 publications

Studies on the Activation Mechanism of Fibrinolytic Enzyme System in Plasma by Human Pancreatic Elastase

Studies on the Activation Mechanism of Fibrinolytic Enzyme System in Plasma by Human Pancreatic Elastase

A Case of Ruptured Hepatoma Followed by Elastase-Induced Disseminated Intravascular Coagulation

Immunochemical Studies of Human Urinary Trypsin Inhibitor

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