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Biomedical subjects

T Sanada

Publications and source records attributed to T Sanada.

At least 55 records · Page 3Linked to original sources
PubMed1987

Isolation and properties of extracellular proteinases from Sporothrix schenckii.

Sporothrix schenckii, mainly in the yeast form of the organism, produced extracellular proteinases when cultivated in liquid media containing albumin or collagen as a nitrogen source, but did not do so in brain heart infusion medium. Isolation of two extracellular proteinases from albumin-containing medium was performed by chromatography on DEAE-Sepharose CL-6B and Sephacryl S-200. Proteinase I had a molecular weight of 36,500, an optimal pH at 6.0, and a pI at 4.8. Despite its activities in weakly acidic conditions, proteinase I demonstrated chymotrypsinlike characteristics, these being indicated by strong inhibitory activity by phenylmethylsulfonyl fluoride and chymostatin and good kinetic constants for a synthetic chymotrypsin substrate, Suc-Ala-Ala-Pro-Phe-MCA. Proteinase II had a molecular weight of 39,000, an optimal pH at 3.5, and a pI at 3.8. Proteinase II showed cathepsin D-like characteristics, these being indicated by strong inhibitory activity by pepstatin, an acidic optimal pH, and good kinetic constants for hemoglobin. These two enzymes hydrolyzed natural substrates such as stratum corneum, type I collagen, and elastin although not type IV collagen. Proteinase production and cell growth in collagen-containing medium and the enzymatic digestion of skin constituents by isolated proteinases suggested that these two proteinases cooperatively enable the organism to invade skin and to obtain peptides from insoluble proteins.

Chromatography, DEAE-Cellulose↗
PubMed1986

Adsorption of plasma proteins to the derivatives of polyaminoetherurethaneurea: the effect of hydrogen-bonding property of the material surface.

Polyaminoetherurethaneureas bearing tertiary amino groups in the main chain (M-PAEUU) were synthesized, quaternized (Q-M-PAEUU) and heparinized (H-M-PAEUU). With increasing portions of diisocyanate and with decreasing portions of polyaminoether in the feed, M-PAEUU containing more hydrogen-bonded urea carbonyl groups was prepared. With increasing hydrogen-bonding character of M-PAEUU, the adsorbed bovine serum albumin (BSA) was more denatured. By quaternization of M-PAEUU, the protein adsorption increased, but the denaturation of adsorbed proteins was suppressed. With increasing ratio of hydrogen-bonded urea carbonyl groups in Q-M-PAEUU, the adsorptions of BSA, bovine serum gamma-globulin (B gamma G), and bovine plasma fibrinogen (BPF) were decreased, but the degree of denaturation of adsorbed proteins was increased. In the adsorption to H-M-PAEUU, both the amount and the degree of denaturation of adsorbed proteins were strongly decreased. The dynamic adsorption experiments of plasma proteins showed the behaviors which are similar to the equilibrium adsorption experiments. The decrease of hydrogen-bonded urea linkages and the increase of hydrophilicity by quaternization and heparinization of the polymer surface may be favorable for building up a hydration layer on the surface, thus suppressing the denaturation of plasma proteins which may trigger blood clotting and thrombus formation.

Adsorption↗