Document Detail


Purification, properties and influence of dietary copper on accumulation and functional activity of lysyl oxidase in rat skin.
MedLine Citation:
PMID:  1674861     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Lysyl oxidase (protein-lysine 6-oxidase; EC 1.4.3.13) is a copper-containing enzyme that functions extracellularly and catalyses the oxidative deamination of peptidyl lysine. Lysyl oxidase was purified 150-175-fold from urea extracts of rat skin and uteri. Features of the enzyme were similar to those reported previously for lysyl oxidase obtained from rat aorta and bovine ligamenture. However, both approximately 40 and approximately 32 kDa polypeptide chains could be isolated from rat skin with apparent lysyl oxidase activity. Antibodies raised in chickens against the approximately 40 kDa form of lysyl oxidase detected the approximately 32 kDa form in immunoblots. Consequently it is inferred that the approximately 32 kDa form of lysyl oxidase is processed from the approximately 40 kDa form of the enzyme. The antibodies were also used to prepare anti(rat lysyl oxidase) affinity columns to facilitate the separation of lysyl oxidase from other proteins in studies to assess the extent to which lysyl oxidase serves as a reservoir for skin copper. At 16 h after an oral dose of copper, as 67Cu, about 6-8% of the total 67Cu incorporated into rat skin was found in association with lysyl oxidase. The lysyl oxidase concentration in rat skin was 2.5-7.5 nmol/g (determined by e.l.i.s.a.). Changing the copper status of rats by feeding a diet deficient in copper did not appear to influence lysyl oxidase accumulation in skin nor the percentage of incorporation of 67Cu in skin as lysyl oxidase. However, when rats were deprived of copper, the functional activity of lysyl oxidase in skin was one-third to one-half the normal values.
Authors:
N Romero-Chapman; J Lee; D Tinker; J Y Uriu-Hare; C L Keen; R R Rucker
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Biochemical journal     Volume:  275 ( Pt 3)     ISSN:  0264-6021     ISO Abbreviation:  Biochem. J.     Publication Date:  1991 May 
Date Detail:
Created Date:  1991-07-03     Completed Date:  1991-07-03     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  657-62     Citation Subset:  IM    
Affiliation:
Department of Nutrition, College of Agricultural and Environmental Sciences, University of California, Davis 95616-8669.
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MeSH Terms
Descriptor/Qualifier:
Animals
Antibody Specificity
Blotting, Western
Copper / deficiency,  metabolism,  pharmacology*
Copper Radioisotopes
Diet
Female
Molecular Weight
Protein-Lysine 6-Oxidase / immunology,  isolation & purification,  metabolism*
Rats
Rats, Inbred Strains
Skin / enzymology*
Urea
Uterus / enzymology
Grant Support
ID/Acronym/Agency:
AM 25358/AM/NIADDK NIH HHS; HD 26777/HD/NICHD NIH HHS; HL 15965/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/Copper Radioisotopes; 57-13-6/Urea; 7440-50-8/Copper; EC 1.4.3.13/Protein-Lysine 6-Oxidase
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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