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Biomedical subjects

O Nishikaze

Publications and source records attributed to O Nishikaze.

At least 37 records · Page 2Linked to original sources
PubMed1983

Characterization of human salivary kallikrein: reactivities to human plasma kininogens and proteinase inhibitors.

In order to clarify the enzymatic properties of human salivary kallikrein, we investigated its actions on human plasma kininogens and response to proteinase inhibitors. Salivary kallikrein released kinin from both LMW and HMW kininogens, but acted preferentially on LMW kininogen. Salivary kallikrein did not completely release the kinin from HMW kininogen even after prolonged incubation (up to 60 min). The kinin releasing activity of salivary kallikrein was not inhibited by plasma proteinase inhibitors such as alpha 2M, alpha 2PI, AT III, and C1 INA after preincubation for 60 min at 37 degrees C, but was inhibited progressively by alpha 1AT as a function of preincubation time. SDS-PAGE revealed that concomitantly with the progressive inhibition a new band of 92,000 daltons, which seemed to be a complex of salivary kallikrein and alpha 1AT, was produced. The kininogen-depleted plasma inhibited the salivary kallikrein to the same degree as alpha 1AT. Therefore, it is suggested that alpha 1AT is the only inhibitor of salivary kallikrein in human plasma.

Humans↗
PubMed1982

The significance of measurements of lipid peroxide and a newly-discovered amidase in inflammation.

Inflammation is a biological defence mechanism against noxious stimuli. Over-strong and oversuppressed inflammatory responses both lead to tissue damage and delay of tissue repair. Determination of inflammatory responses on the basis of chemical mediators, however, only informs about the degree of these responses themselves. It cannot show whether these responses are over-strong or oversuppressed. We have developed a prototype standard for safe judgement of the appropriateness of inflammatory responses: measurements of lipid peroxide (a product of tissue damage) and a newly-discovered amidase (related to wound healing).

Amidohydrolases↗
PubMed1981

Kininogen and kallikrein in saliva of periodontally-diseased subjects.

The kininogen level in saliva was measured by radioimmunoassay, and the kallikrein activity was determined by an enzymatic method with D-Val-Leu-Arg-p-nitroanilide. The kininogen level in the Periodontally-diseased Group was remarkably high compared with that of the Periodontally-healthy Group, but the kallikrein activity was approximately the same in the two groups.

Adult↗
PubMed1981

Antiplasmin activity in carrageenin-induced inflammation of rats.

The significance of inhibitors in the coagulation-fibrinolysis system was examined by inducing experimental inflammation with carrageenin. Fast-acting plasmin inhibitor, alpha 2-plasmin inhibitor (alpha 2-Pl), was recently discovered in human blood and it was stated that such alpha 2-Pl represents the most sensitive and specific inhibitor of plasmin. The possible role of alpha 2-Pl has been studied in detail in vitro and in vivo in relation to the thrombolytic condition and bleeding based on hyperfibrinolysis. However, the significance of alpha 2-Pl has not been clarified for the inflammatory state and diseases. In the present study in order to clarify the possible role of alpha 2-Pl in inflammatory responses, the antiplasmin activity in the plasma and local fluid (exudate) was investigated using an animal model of inflammation. After subcutaneous injection of carrageenin into the dorsum of rats, on day 7 and 21, the antiplasmin activity in the plasma was significantly higher than that in the plasma of non-treated rats (p less than 0.001). However, the antiplasmin activity in the plasma on day 7 was not significantly different from that on day 21. On the other hand, the antiplasmin activity in the exudate on day 21 was significantly lower than that on day 7 (p less than 0.001). Based on ;these results, it is suggested that the antiplasmin in the inflammatory exudate was consumed during the inflammation to form the hard wall of the carrageenin pouch.

Animals↗
PubMed1980

Alpha 1-antitrypsin and alpha 2-macroglobulin do not inhibit the kinin-releasing activity of kallikreins from human urine and saliva.

Alpha 1-Antitrypsin, alpha 2-macroglobulin and low-molecular weight kininogen were isolated from human serum and kallikreins from human urine and saliva. Alpha 1-antitrypsin and alpha 2-macroglobulin inhibited the activity of trypsin in releasing kinin from low-molecular weight kininogen, due to their binding with the enzyme, but did not inhibit or bind with urinary and salivary kallikreins.

Humans↗
PubMed1979

Purification and immunochemical properties of human low molecular weight kininogen.

A low molecular weight (LMW) kininogen was isolated from pooled human serum by chromatography on DEAE-Sephadex A-50, CM-Sephadex C-50, Sephadex G-150, and Sephadex G-100. It was shown to be homogeneous by ultracentrifugation, polyacrylamide gel electrophoresis, and immunoelectrophoresis. The sedimentation coefficient, S020,W, of purified LMW kininogen was 3.85 s, and its molecular weight was determined to be 78,000 by Sephadex G-100 gel-filtration. The LMW kininogen contained 79.3% protein, 8.0% hexose, 3.9% hexosamine, and 4.9% sialic acid. In order to determine the immunochemical properties of LMW kininogen, specific antiserum was prepared in rabbits. The antigenic determinant of LMW kininogen was not related to the sialic acid and kinin moieties in the kininogen molecule, but could not be distinguished from that of high molecular weight (HMW) kininogen. In the quantitative single radial immunodiffusion test, a sialic acid-free LMW kininogen reacted to a greater extent with the antiserum than the native LMW kininogen. The kininogen level in human serum was estimated by single radial immunodiffusion. The antiserum cross-reacted with monkey serum, but not with sera from dogs, rats, and mice, horses, pigs, guinea pigs, oxen, and rabbits.

Chromatography, Affinity↗
PubMed1979

Removal of contaminating substances before gas-liquid-chromatographic determination of aldosterone in urine.

This paper deals with removal of contaminants before gas-chromatographic determination of aldosterone in urine. Urine is incubated with beta-glucuronidase, which hydrolyzes all beta-glucuronides except aldosterone-18-glucuronide. The contaminants (the aglycones released and other methylene chloride-soluble substances) are extracted with methylene chloride. Solvolysis of the aqueous phase liberates aldosterone from aldosterone-18-glucuronide, which then is extracted with methylene chloride and oxidized by use of periodic acid. The resulting lactone can be easily separated by one-dimensional thin-layer chromatography and determined by gas-liquid chromatography.

Aldosterone↗
PubMed1979

New micro-turbidimetric method for determination of protein in cerebrospinal fluid and urine.

We report a new micro-scale (0.1-mL sample) turbidimetric method for determination of protein by use of benzethonium chloride in alkali. The method is highly specific for protein, has a higher sensitivity than the classic method of Lowry et al., and shows satisfactory reproducibility and recovery. The turbidity produced in our method is the same for albumin and gamma-globulin and is more stable than in Meulemans' method (in which sulfosalicylic acid is used) or in the method of Bossak et al. (in which trichloracetic acid is used). In contrast to Pesce and Strande's method, there is no manipulative loss of protein.

Benzethonium↗
PubMed1977

Hydrolysis of steroid glucuronides with beta-glucuronidase preparations from bovine liver, Helix pomatia, and E. coli.

We determined the enzymic activity of beta-glucuronidase preparations from bovine liver, Helix pomatia, and Escherischia coli with steroid glucuronides and nonsteroid glucuronides as substrates. We also studied the effect of Na2SO4 on the enzymic hydrolysis of several substrates with the three preparations of beta-glucuronidase. Na2SO4 increases the rate of hydrolysis of all substrates with beta-glucuronidase from bovine liver. Hydrolysis of a steroid glucoronide with beta-glucuronidase from Helix pomatia and E. coli is inhibited by Na2SO4. None of the three enzyme preparations gives complete hydrolysis of urinary steroid conjugates, because urine contains inhibitors, which can be removed by absorption chromatography of the urine on a column of neutral polystyrene resin Amberlite XAD-2. But when Amberlite XAD-2 is not used, hydrolysis of urinary glucuronides of androsterone, etiocholanolone, pregnanediol, estriol, and 17-hydroxycorticosteroids proves that, given an incubation time of 24 h, the beta-glucuronidase preparation from bovine liver, in the presence of Na2SO4, is suited for determining all of the above steroids except esriol; the preparation from Helix pomatia is good for determining estriol and 17-hydroxycorticosteroids; the preparation from E. coli is good for determining androsterone, 17-hydroxycorticosteroids, and especially estriol, the glucuronide, of which is maximally hydrolyzed in 2 h.

17-Hydroxycorticosteroids↗
PubMed1977

Improved hydrolysis of urinary 17-hydroxycorticosteroid glucuronides with beta-glucuronidase from Helix pomatia, on adding sodium sulfate.

Sodium sulfate increases the hydrolysis of urinary 17-hydroxycorticosteroid glucuronides with beta-glucuronidase preparations derived from Helix pomatia because it removes the inhibitory activity of urinary high-molecular-weight substances. For maximum hydrolysis of urinary 17-hydroxycorticosteroid glucuronides, the hydrolysis [5 ml of urine, 0.5 ml of 2 mol/liter acetate buffer (pH 5.0)] should be conducted in the presence of sodium sulfate (final concentration: 80 g/liter) with (a) 600 Fishman units of the enzyme per milliliter of urine (18 h at 52 degrees C) or (b) with 1500 units of the enzyme per milliliter of urine (3 h at 57 degrees C). Under conditions a, analytical recovery of steroid glucuronides added to 12 urine samples was 99 +/- 2.1% (96-102%). Values obtained for 20 urine samples with this method were 99 +/- 2.7% (93-104%) as great as those yielded by a method in which 600 units of the enzyme from bovine liver are used together with sodium sulfate (18 h at 48 degrees C).

17-Hydroxycorticosteroids↗
PubMed1976

Immunochemical study of beta-glucuronidase inhibitor from porcine sublingual gland. Relationship between the antigenic determinant and the active site of the inhibitor.

Following removal of sialic acid by neuraminidase treatment the activity of the beta-glucuronidase inhibitor was remarkably decreased, but the antigenic determinant was not affected. A partial common antigen to the inhibitor was isolated from porcine small intestine, by successive fractionation of trypsin extraction of the latter on Sephadex G-150, DEAE-cellulose and Sepharose 4B column chromatography. The immunologic and characteristic properties of the common antigen were compared with those of the beta-glucuronidase inhibitor is not identical with its antigenic determinant.

Animals↗
PubMed1975

[Decomposition of steroids during incubation with beta-glucuronidase and during storage of urine].

Androsterone, etiocholanolone, pregnanetriol, dehydroepiandrosterone, pregnanediol, tetrahydrocortisol, 5-pregnenolone and 11-beta-OH-androsterone were incubated with beta-glucuronidase preparations (Helix pomatia, bovine liver and E. coli) for 96 hrs at 37 degrees C. After extraction and silylation they were gas-chromatographed. The first 3 steroids were left practically intact. The least decomposition of the last 5 steroids occurred with the liver enzyme. Testosterone and 11-ketoandrosterone without the enzymes showed 74 and 35% recoveries. Cortisol and tetrahydrocortisol, incubated with the first two enzymes for 18 hrs at 37 degrees and 48 degrees C, showed nearly 100% recoveries. The recoveries of 17-OHCS in urines (pH 7.8-8.8), stored for 7 days, was 80% at 20 degrees-25 degrees C and 55% at 25 degrees-30 degrees C. The same samples, brought to pH 1.8-2.8 WITH NaHSO4 before the storage, showed a 100% recovery.

17-Hydroxycorticosteroids↗