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dc.contributor.authorJacobson, LA,
dc.contributor.authorJen-Jacobson, L
dc.contributor.authorHawdon, JM
dc.contributor.authorOwens GP, GP
dc.contributor.authorShah, MV
dc.contributor.authoret al
dc.date.accessioned2013-06-10T14:29:37Z
dc.date.available2013-06-10T14:29:37Z
dc.date.issued1988
dc.identifier.citationGenetics. 1988 Jun;119(2):355-63.en
dc.identifier.uriwww.ncbi.nlm.nih.gov/whalecom0/pubmed/3396869
dc.identifier.urihttp://erepository.uonbi.ac.ke:8080/xmlui/handle/123456789/30991
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC1203418/
dc.description.abstractMutants of Caenorhabditis elegans having about 10% of wild-type activity of the aspartyl protease cathepsin D have been isolated by screening. Mutant homozygotes have normal growth rates and no obvious morphological or developmental abnormalities. The mutant gene (cad-1) has been mapped to the right extremity of linkage group II. Heterozygous animals (cad-1/+) show intermediate enzyme levels and animals heterozygous for chromosomal deficiencies of the right extremity of linkage group II have 50% of wild-type activity. Cathepsin D purified from a mutant strain has a lower activity per unit mass of pure enzyme. These data suggest that cad-1 is a structural gene for cathepsin D.en
dc.language.isoenen
dc.titleIdentification of a putative structural gene for cathepsin D in Caenorhabditis elegans.en
dc.typeArticleen
local.publisherDepartment of Biological Sciences, University of Pittsburgh, Pennsylvania 15260.en


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