Cheryl R. Kuhn , Ryno J. Naudé , James Travis , Willem Oelofsen
{"title":"The isolation and partial characterization of α1-proteinase inhibitor from the serum of the ostrich (struthio camelus)","authors":"Cheryl R. Kuhn , Ryno J. Naudé , James Travis , Willem Oelofsen","doi":"10.1016/0020-711X(94)90114-7","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Native and cleaved α<sub>1</sub>-proteinase inhibitor was purified from ostrich serum using Sepharose-blue dextran chromatography, ammonium sulfate precipitation and ion exchange chromatography on DEAE-Toyopearl 650 M at pH 8.8 and 6.5.</p></span></li><li><span>2.</span><span><p>2. Ostrich α<sub>1</sub>PI displayed M<sub>r</sub> values of 68,100 using gradient PAGE and 66,200 using Ferguson plots.</p></span></li><li><span>3.</span><span><p>3. Isoelectric focusing of ostrich α<sub>1</sub>-PI in the pH range 3–10 revealed pi values of 4.84 and 4.91, and in the pH range 4–6 the characteristic microheterogeneity observed for mammalian α<sub>1</sub>-PIs was displayed.</p></span></li><li><span>4.</span><span><p>4. The presence of sialic acid, hexoses and hexosamines was detected using chemical methods, but were found in much lower quantities as compared to α<sub>1</sub>-PIs of other species.</p></span></li><li><span>5.</span><span><p>5. Western blot analysis demonstrated a positive reaction between the native and cleaved ostrich α<sub>1</sub>-PIs and the antibodies to the ostrich α<sub>1</sub>-PIs raised in rabbits. No cross-reactivity was demonstrated by Western blot analysis between human α<sub>1</sub>-PI and antibodies to ostrich α,-PI.</p></span></li><li><span>6.</span><span><p>6. The inhibitory effect of α<sub>1</sub>-PI on elastase and chymotrypsin was also investigated.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 6","pages":"Pages 843-853"},"PeriodicalIF":0.0000,"publicationDate":"1994-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90114-7","citationCount":"7","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"International Journal of Biochemistry","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0020711X94901147","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 7
Abstract
1.
1. Native and cleaved α1-proteinase inhibitor was purified from ostrich serum using Sepharose-blue dextran chromatography, ammonium sulfate precipitation and ion exchange chromatography on DEAE-Toyopearl 650 M at pH 8.8 and 6.5.
2.
2. Ostrich α1PI displayed Mr values of 68,100 using gradient PAGE and 66,200 using Ferguson plots.
3.
3. Isoelectric focusing of ostrich α1-PI in the pH range 3–10 revealed pi values of 4.84 and 4.91, and in the pH range 4–6 the characteristic microheterogeneity observed for mammalian α1-PIs was displayed.
4.
4. The presence of sialic acid, hexoses and hexosamines was detected using chemical methods, but were found in much lower quantities as compared to α1-PIs of other species.
5.
5. Western blot analysis demonstrated a positive reaction between the native and cleaved ostrich α1-PIs and the antibodies to the ostrich α1-PIs raised in rabbits. No cross-reactivity was demonstrated by Western blot analysis between human α1-PI and antibodies to ostrich α,-PI.
6.
6. The inhibitory effect of α1-PI on elastase and chymotrypsin was also investigated.
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