title: C1q, a collagen-like complement subcomponent, in dermatosparactic cattle: its extracellular modification is not affected by lack of procollagen N-terminal proteinase (pN-proteinase).
abstract: C1q, a collagen-like complement protein, was purified from the serum of a dermatosparactic calf which lacks procollagen N-terminal proteinase (pN-proteinase). The specific hemolytic activity of the serum C1q from the dermatosparactic animal was identical to that of C1q from a normal calf. Gel-filtration of serum from the dermatosparactic calf, on Sepharose 6B, showed the presence of C1q-antigenic material at only one position which was identical to the elution position of normal bovine C1q. No difference, under dissociating conditions, could be seen in the size of the chains of C1q in specific immunoprecipitates isolated from the sera of dermatosparactic and normal animals, as judged by polyacrylamidegel electrophoresis (PAGE) in the presence of sodium dodecyl sulfate (SDS). The C1q from the dermatosparactic animal showed the same N-terminal amino acid and tryptic-digest peptide pattern on HPLC as C1q from the normal calf. These results strongly suggest that pN-proteinase is not involved in the extracellular processing of C1q.
authors: Department of Bacteriology, Nara Medical College, Kashihara, Japan.
authors: K
authors: K
authors: Yonemasu
authors: T
authors: T
authors: Sasaki
authors: Y
authors: Y
authors: Dohi
authors: C M
authors: CM
authors: Lapière
authors: B
authors: B
authors: Nusgens
mesh_terms: D000818:Animals; D002417:Cattle; D002418:Cattle Diseases / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D015922:Complement C1q / Q000378:metabolism*; D010449:Peptide Mapping; D011233:Precipitin Tests; D011348:Procollagen N-Endopeptidase / Q000378:metabolism*; D012871:Skin Diseases / Q000662:veterinary*
chemical_list: D015922:Complement C1q; D011348:Procollagen N-Endopeptidase