| pubmed-article:5289249 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:5289249 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:5289249 | lifeskim:mentions | umls-concept:C0033235 | lld:lifeskim |
| pubmed-article:5289249 | lifeskim:mentions | umls-concept:C0033237 | lld:lifeskim |
| pubmed-article:5289249 | lifeskim:mentions | umls-concept:C0765250 | lld:lifeskim |
| pubmed-article:5289249 | lifeskim:mentions | umls-concept:C0242414 | lld:lifeskim |
| pubmed-article:5289249 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:5289249 | pubmed:dateCreated | 1972-3-6 | lld:pubmed |
| pubmed-article:5289249 | pubmed:abstractText | A heritable connective tissue disorder of cattle, dermatosparaxis, is characterized by an extreme fragility of the skin and the presence of additional peptides at the N-terminal extremities of the collagen alpha chains, p-alpha(1) and p-alpha(2). The existence of an enzyme activity is demonstrated in normal connective tissues that is capable of cleaving these additional N-terminal peptides from dermatosparaxic collagen. The activity is demonstratable with dermatosparaxic collagen in solution, as well as with reconstituted dermatosparaxic collagen fibrils polymerized in vitro. It has a pH optimum of about 7.0 and is inhibited by EDTA and mercaptoethanol. Differences in K(m) and V(max) values exist depending on the substrate utilized, i.e., p-alpha(1) or p-alpha(2); and the presence of additional amounts of one substrate, p-alpha(1), alters the concentration requirement for the second substrate, p-alpha(2). The product of the excision reaction with p-alpha(1) as substrate is an equimolar amount of normal alpha(1) monomer; the product when p-alpha(2) is substrate is an equimolar amount of normal alpha(2) monomer. The enzyme is present in normal calf skin, tendon, aorta, cartilage, and lung; it can be demonstrated in the skin of rats and humans. The enzyme activity is absent in dermatosparaxic connective tissues, thus suggesting that dermatosparaxis is caused by the absence of a normal enzyme function rather than by the production of an abnormal collagen. | lld:pubmed |
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| pubmed-article:5289249 | pubmed:language | eng | lld:pubmed |
| pubmed-article:5289249 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:5289249 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:5289249 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:5289249 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:5289249 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:5289249 | pubmed:author | pubmed-author:KohnL DLD | lld:pubmed |
| pubmed-article:5289249 | pubmed:author | pubmed-author:LenaersAA | lld:pubmed |
| pubmed-article:5289249 | pubmed:author | pubmed-author:LapièreC MCM | lld:pubmed |
| pubmed-article:5289249 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:5289249 | pubmed:volume | 68 | lld:pubmed |
| pubmed-article:5289249 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:5289249 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:5289249 | pubmed:pagination | 3054-8 | lld:pubmed |
| pubmed-article:5289249 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:5289249 | pubmed:year | 1971 | lld:pubmed |
| pubmed-article:5289249 | pubmed:articleTitle | Procollagen peptidase: an enzyme excising the coordination peptides of procollagen. | lld:pubmed |
| pubmed-article:5289249 | pubmed:publicationType | Journal Article | lld:pubmed |
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