ABSTRACT
Immunobiologic activities of tuberculin preparations and their components have been comparatively studied using gel filtration and high-performance liquid chromatography (HPLC) techniques. It is shown that high-molecular weight fraction of protein-purified derivate tuberculin (PPD) had higher activity as compared to nonfractionated preparation in skin tests on guinea pigs sensitized with Mycobacterium bovis BCG as well as in enzyme-linked immunosorbent assay with affinity purified rabbit antibodies against PPD. Using the preparative HPLC-technique we failed to isolate a component of PPD having greater tuberculin test potency than nonfractionated preparation.
Subject(s)
Tuberculin/analysis , Animals , Chromatography, Gel , Chromatography, High Pressure Liquid , Enzyme-Linked Immunosorbent Assay , Guinea Pigs , Molecular Weight , Mycobacterium bovis/immunology , Tuberculin/immunology , Tuberculin TestABSTRACT
Collagen I was isolated from human bone tissue and from mice bone tissue of the AKR-50 strain at the pronounced stage of leukosis. Dissimilarity of native and leukemic collagens was exhibited after evaluation of their amino acid composition, electrophoretic mobility in polyacrylamide gel containing SDS, content of the carbohydrate moiety as well as of isopoints, elution profiles in reverse-phase chromatography and gel filtration and electron microscopy of SLS-crystallites. Impairments of collagen processing in leukemia appear to be responsible for its alterations in structure and properties.
Subject(s)
Collagen/chemistry , Precursor Cell Lymphoblastic Leukemia-Lymphoma/metabolism , Adolescent , Amino Acids/chemistry , Animals , Child , Child, Preschool , Chromatography, High Pressure Liquid , Collagen/ultrastructure , Electrophoresis, Polyacrylamide Gel , Humans , Infant , Isoelectric Focusing , Mice , Mice, Inbred AKR , Precursor Cell Lymphoblastic Leukemia-Lymphoma/pathologyABSTRACT
Type I collagen in skin of rats who were given redundant amounts of leucin, valine, methionine or phenyl alanine differed essentially from the normal level in the amino acidic composition. Considerable shifts in the value of pI of the proteins under study as compared with the normal level are found during isofocusing. When studying subunits of collagen preparations by the reverse-phase chromatography certain differences typical of each studied state are revealed in the elution profiles in normalcy and under amino acid loadings.
