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Results for “Brinolase”

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At least 19 recordsLinked to original sources
PubMed1977

Fungal proteases and the mammalian kinin system: I. Brinolase-catalyzed kinin formation and S2160 hydrolysis.

Brinolase, a fungal protease advocated for thrombolytic therapy, released kinin peptides from semi-purified kininogens of the human, rabbit, guinea pig, and mouse, and moreover cleaved an arginyl bond of the chromogenic peptide S2160. Its kinetics demonstrated marked differences from the mammalian protease trypsin. Whereas trypsin liberated 100% of the available kinin in 30 min at pH 8, brinolase generated a maximum of only 22% under optimal conditions, viz. incubation of 5 microgram/ml enzyme at pH 4.7 for 5 min. Longer incubations yielded less detectable kinin. This maximal release at acidic pH was not due to increased kininogen consumption, nor was it inhibited by the acid protease inhibitor pepstatin. Evidence is presented that brinolase, unlike trypsin, might both release and destroy kinins.

Anilides↗
PubMed1976

Effect of brinolase on corneal endothelium.

We investigated Brinolase, a substance producing enzymatic zonulysis, for effects on the physiological and anatomical function of the corneal endothelium in the specular microscope. Concentrations of 100 C2 units/ml perfused for ten minutes did not appear to damage the corneal endothelium. Longer perfusions or higher concentrations possibly produced alterations in the physiological functions of the endothelium, but no significant anatomic change was demonstrated. Longer perfusion times with high concentrations (1,600 C2 units/ml) resulted in the formation of holes which perforated the corneal stroma.

Animals↗
PubMed1979

Clinical trial of brinase and anticoagulants as a method of treatment for advanced limb ischemia.

A randomized, single-blind trial of repeated intravenous infusion of Brinase was carried out in 70 petients with severe chronic limb ischemia, who were candidates for lumbar sympathectomy or amputation. The enzyme caused s significant increase in calf and ankle pressure index. At six months follow-up, the clinical results were statistically significant in favour of Brinase when all patients were considered, but not if 10 patients with Buerger's disease were omitted from the analysis. Patients treated with a combination of Brinase and coumarins had a better clinical outcome than patients receiving either treatment on its own.

Aged↗
PubMed1987

Studies of protease and protease inhibitors in familial amyloidotic polyneuropathy.

Serum levels of 6 protease inhibitors, alpha 1-antitrypsin, Cl inactivator, alpha 2-macroglobulin, antithrombin-3, alpha 1-antichymotrypsin and inter-alpha-trypsin inhibitor were measured in patients with familial amyloidotic polyneuropathy (FAP) and a control group without neurologic disease. No significant differences were observed between the 2 groups. The proteolytic effect of brinase, an enzyme from Aspergillus oryzae, on amyloid tissue sections from patients with FAP was also evaluated. Amyloid fibrils were degraded by brinase, while the tissue structure remained fairly intact.

Amyloid↗
PubMed1988

Properties of the complex between alpha 2-macroglobulin and brinase, a proteinase from Aspergillus oryzae with thrombolytic effect.

The proteinase, brinase (Mr approximately 35000), from Aspergillus oryzae, which has been used in therapeutic attempts as a thrombolytic agent in arterial thrombosis, binds to purified human alpha 2-macroglobulin (alpha 2M) with a stoichiometry of 1.7-1.9 mol of enzyme/mol inhibitor. This binding leads to quantitative cleavage of the bait region of the inhibitor and to release of 3.6 thiol groups per molecule of alpha 2M, reflecting cleavage of the thioester bonds. The reaction with brinase is accompanied by a similar conformational change of alpha 2M as the reaction with trypsin, as shown by gradient gel electrophoresis and spectroscopic analyses. Brinase thus binds to alpha 2M in a similar manner as most small proteinases. However, in the complex formed at saturation of alpha 2M with brinase, the enzyme retains considerable proteolytic activity against macromolecular substrates, corresponding to about 25% of that of the free enzyme with fibrin as substrate. This finding indicates that the trapping of brinase by alpha 2M is less efficient than that of smaller proteinases. The complex formed at equimolar concentrations of the reactants has appreciably lower, although still significant, activity, amounting to 5-10% of that of free brinase against fibrin. This proteolytic activity of alpha 2M-brinase complexes against high-molecular-weight substrates most likely accounts for the thrombolytic effect of brinase in vivo. The observations also indicate that this thrombolytic activity increases more than proportionally to the brinase concentration as the latter is increased to approach saturation of alpha 2M in plasma.

Animals↗
PubMed1982

Total and surface-located sialic acid levels in normal and leukaemic lymphocytes: relationship to T and B cell nature and to location in vivo.

Unfractionated normal blood lymphocytes (predominantly T lymphocytes) showed significantly elevated total and neuraminidase-susceptible sialic acid compared with CLL lymphocytes (predominantly B lymphocytes). T-enriched fractions from normal blood contained about three-fold the sialic acid content of the corresponding T-depleted fractions, and similarly low values were also obtained for T-depleted fractions from tonsils. Thus the reduced sialic acid levels in CLL lymphocytes appear to be due to their B cell nature. In contrast to the situation in normal peripheral venous blood, tonsillar T and B cells did not differ markedly in sialic acid content, suggesting that for T cells maturity and/or location in vivo are important determinants of this parameters. Results with calf thymocytes were in agreement with this. Sialic acid was estimated in malignant B and T lymphoblasts. Shedding of sialic acid-containing moieties from lymphocytes was also examined.

B-Lymphocytes↗