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Biomedical subjects

M Ohi

Publications and source records attributed to M Ohi.

At least 109 records · Page 6Linked to original sources
PubMed1986

Analysis by electrophoretic transfer blotting of Japanese cedar pollen allergens which react with IgG and IgE antibodies in the serum of patients.

Crude extract of Japanese cedar pollen was fractionated by DEAE-cellulose chromatography to separate the major allergenic components. In order to analyze which antigens react with IgG or IgE antibodies in the serum of Japanese cedar pollinosis patients, an electrophoretic transfer blotting was performed. Both IgE and IgG antibodies reacted with several common antigens, while IgG additionally reacted with some low-molecular-weight proteins.

Adolescent↗
PubMed1986

Proteolytic activity and serum protease inhibitors in nasal secretions from adult patients with common colds.

Proteolytic activity and concentrations of serum protease inhibitors were measured in nasal secretions collected from 14 adult patients (6 males and 8 females) with common colds. Elastase concentration and fibrinolytic activity increased about three days after the onset of the colds, and there was a significant correlation between both values (p less than 0.01). Trypsin-like protease activity was very low. Of all serum protease inhibitors, inter-alpha-trypsin inhibitor could not be detected, and alpha 2-macroglobulin could be detected in only two cases. Variation of alpha 1-antitrypsin value was very similar to that of alpha 1-antichymotrypsin, and there was a significant correlation between alpha 1-antitrypsin and elastase (p less than 0.001). Phoretic patterns of crossed immuneelectrophoresis revealed the presence of alpha 1-antitrypsin-protease complex. alpha-protease inhibitors are major serum protease inhibitors in nasal secretions of persons with colds, and inhibit excess proteolytic activity of serine proteases. This protection is considered to be one of the major factors in preventing irreversible mucosal change.

Adult↗
PubMed1986

Significance of lysosomal proteases; cathepsins B and H in maxillary mucosa and nasal polyp with non-atopic chronic inflammation.

Tissue extracts from maxillary mucosa (MM) and nasal polyp (NP) with non-atopic chronic inflammation were applied to DEAE-Sepharose, and hydrolytic activity of lysosomal proteases (cathepsins B and H) was measured by the fluorometric assay. Hydrolytic activity of cathepsins B and H in MM, of which cathepsin B was a major one, was about 3.5 times as high as that in NP. Protein composition resembled in both extracts except for several apparent protein bands with high molecular weight observed in NP. These results suggest that in MM with chronic inflammation, mucosal destruction induced by excess lysosomal granuloproteases overwhelming protease inhibitors would occur, being much related to the formation of its irreversible lesion.

Cathepsin B↗
PubMed1985

Purification and characterization of tissue-type plasminogen activator in maxillary mucosa with chronic inflammation.

Tissue-type plasminogen activator (TPA) was purified from maxillary mucosa with chronic inflammation and compared with urokinase. Purification procedure consisted of the extraction from delipidated mucosa with 0.3M potassium acetate buffer (pH 4.2), 66% saturation of ammonium sulfate, zinc chelate-Sepharose, concanavalin A-Sepharose and Sephadex G-100 gel filtration chromatographies. The molecular weight of the TPA was approximately 58,000 +/- 3,000. Its activity was enhanced in the presence of fibrin and was quenched by placental urokinase inhibitor, but not quenched by anti-urokinase antibody. The TPA made no precipitin line against anti-urokinase antibody, while urokinase did. All these findings indicate that the TPA in maxillary mucosa with chronic inflammation is immunologically dissimilar to urokinase and in its affinity for fibrin.

Adult↗
PubMed1985

Partial purification and characterization of the tissue plasminogen activator in nasal mucosa and nasal polyp.

Tissue plasminogen activator was partially purified from the inferior turbinate and nasal polyp, and its biochemical properties were investigated. Similar TPA peak positions were seen in the gel filtration chromatography of both tissues, and the molecular weight was approximately 65,000, which was comparable to TPA of pig heart (55,000-60,000). Activity of TPA from inferior turbinate was higher than that from nasal polyp. TPA from both tissues was completely inhibited by trans-aminomethyl cyclohexane carboxylic acid, dithiothreitol, and diisopropylfluorophosphate and had similar inhibition profiles to TPA from pig heart. All these findings indicate that TPA from both tissues is undoubtedly a plasminogen-activating enzyme and serine-type protease and would be biochemically identical.

Chromatography, Gel↗
PubMed1985

Purification of glandular kallikrein in maxillary mucosa from humans suffering from chronic inflammation.

Glandular kallikrein was purified from human maxillary mucosa with chronic inflammation and its biochemical properties were characterized. The purification procedure consisted of extraction with 3 mol/l KCl, saturation of ammonium sulfate (66%), DEAE-Sepharose, arginine-Sepharose and Sephadex G-150 chromatographies. Maxillary mucosa with chronic inflammation contains considerable activity of glandular kallikrein, which is a serine protease with limited proteolytic activity and its biochemical properties resemble those of pancreatic kallikrein.

Adult↗
PubMed1984

Antifibrinolytic activity in middle ear effusion.

No activity of the plasmin and plasminogen activators could be detected in middle ear effusion (MEE). A streptokinase proactivator, which was not plasminogen and markedly enhanced the activation of plasminogen by streptokinase, could be detected. MEE had an apparent inhibitory activity against both thiol protease (papain) and serine proteases (plasmin and trypsin). All these findings indicate that MEE contains unsaturated protease inhibitors and is in a state of predominance of inhibitors over fibrinolytic activity.

Antifibrinolytic Agents↗
PubMed1984

Effect of ipratropium bromide on nasal mucociliary transport.

Ipratropium bromide is a parasympatholytic drug. After application to the nose, the nasal mucociliary transport time was measured using the method of the saccharin test. This compound did not cause any changes in the nasal mucociliary transport function.

Administration, Intranasal↗