| pubmed-article:16667694 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16667694 | lifeskim:mentions | umls-concept:C1095831 | lld:lifeskim |
| pubmed-article:16667694 | lifeskim:mentions | umls-concept:C0004755 | lld:lifeskim |
| pubmed-article:16667694 | lifeskim:mentions | umls-concept:C2717970 | lld:lifeskim |
| pubmed-article:16667694 | lifeskim:mentions | umls-concept:C0205164 | lld:lifeskim |
| pubmed-article:16667694 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:16667694 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:16667694 | lifeskim:mentions | umls-concept:C0868946 | lld:lifeskim |
| pubmed-article:16667694 | lifeskim:mentions | umls-concept:C2350166 | lld:lifeskim |
| pubmed-article:16667694 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:16667694 | pubmed:dateCreated | 2010-6-29 | lld:pubmed |
| pubmed-article:16667694 | pubmed:abstractText | We previously described the purification and characterization of a 37,000 M(r) cysteine proteinase, designated EP-A, from gibberellic acid (GA(3))-induced barley (Hordeum vulgare L.) aleurone layers (S Koehler, T-HD Ho [1988] Plant Physiol 87: 95-103). A second, more abundant protease has now been purified from this tissue. This protease, designated EP-B, has an apparent M(r) of 30,000 on 10% sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). It resolves into two bands during native isoelectric focusing with pl of 4.6 to 4.7. The analysis of hemoglobin digestion products by both gradient SDS-PAGE and Bio-Gel P2 chromatography, the inhibition of protease activity by E-64, leupeptin, iodoacetate, and p-hydroxymercuribenzoate, and N-terminal amino acid sequence analysis all indicate that EP-B is a cysteine proteinase. The first 22 amino acids at the N terminus of EP-B have been determined, and their sequence is 90% similar to that of EP-A. EP-B has properties similar to EP-A; however, EP-B is much more sensitive to high pH during gel electrophoresis and therefore is not detectable on native activity gels used to detect EP-A. Its pH optimum against azocasein and hemoglobin is 4.5 to 4.6. Both of these proteinases digest hordeins enriched for the B and D fractions into similar peptides of 25,000 to 2,000 M(r) as determined by gradient SDS-PAGE. | lld:pubmed |
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| pubmed-article:16667694 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16667694 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16667694 | pubmed:status | PubMed-not-MEDLINE | lld:pubmed |
| pubmed-article:16667694 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:16667694 | pubmed:issn | 0032-0889 | lld:pubmed |
| pubmed-article:16667694 | pubmed:author | pubmed-author:HoT HTH | lld:pubmed |
| pubmed-article:16667694 | pubmed:author | pubmed-author:KoehlerS MSM | lld:pubmed |
| pubmed-article:16667694 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16667694 | pubmed:volume | 94 | lld:pubmed |
| pubmed-article:16667694 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16667694 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16667694 | pubmed:pagination | 251-8 | lld:pubmed |
| pubmed-article:16667694 | pubmed:dateRevised | 2010-9-15 | lld:pubmed |
| pubmed-article:16667694 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:16667694 | pubmed:articleTitle | A major gibberellic Acid-induced barley aleurone cysteine proteinase which digests hordein : purification and characterization. | lld:pubmed |
| pubmed-article:16667694 | pubmed:affiliation | Department of Biology, Plant Biology Program, Washington University, St. Louis, Missouri 63130. | lld:pubmed |
| pubmed-article:16667694 | pubmed:publicationType | Journal Article | lld:pubmed |
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