PubMed Health⌕ Search

Biomedical subjects

S Krantz

Publications and source records attributed to S Krantz.

At least 73 records · Page 4Linked to original sources

[Electrophoretic patterns of differently prepared fibrinogen subunits in sodium dodecyl sulfate containing polyacrylamide gels].

The electrophoretic behaviour of mercapto, carboxamidomethyl, carboxymethyl and thiosulfonic acid derivatives of rabbit fibrinogen subunits was investigated electrophoretically in sodium dodecyl sulfate containing polyacrylamide gels. Comparing carboxymethyl, carboxamidomethyl and thiosulfonic acid derivatives with the corresponding mercapto subunits divergent electrophoretic patterns were observed. Especially, the position of the Bbeta-chain was strongly dependent on the method of preparation. Similar results were obtained from investigating electrophoretic mobilities of albumin with differently substituted SH-groups after reduction with mercaptoethanol.

Albumins↗

[Chemical properties of plasma fibrinogens and fibrins from normal and cobalt-treated rabbits].

The sulfitolysis products of fibrinogens from normal and cobalt-treated rabbits (5 mg Co2+/kg b.w.) were resolved by ion exchange chromatography on CM-cellulose columns. The elution patterns of both fibrinogens showed a distinct heterogeneity of gamma-chains. Furthermore, a gamma-chain derivative from cobalt fibrinogen could be distinguished electrophoretically from the corresponding one of normal fibrinogen because of its reduced electrophoretic mobility. Normal and cobalt fibrinogen did not differ from each other in their N-terminal (Val2 Ala2 Tyr2) and C-terminal (Pro1-2 Val4-5) amino acid compositions related to a subunit structure of A alpha 2 B beta 2 gamma 2, and their carbohydrate contents - neutral hexoses 1,21% (1,26%), N-acetyl hexosamines 1,16% (1,05%), N-acetyl neuraminic acid 1,19% (1, 13%), values for cobalt fibrinogen in parentheses. The main amounts of carbohydrates are bound to gamma- and B beta-chains, The BrCn cleavage products from cobalt fibrinogen and its gamma- and B beta-chains showed other electrophoretic properties than the corresponding derivatives from normal fibrinogen. But BrCN split products of A alpha-chains of both fibrinogens were electrophoretically very similar. Spectrographic investigations of the S-sulfoderivates demonstrated a diminution of the absorption maximum near 282mn of gamma and B beta derivatives of cobalt fibrinogen. A alpha-chains of both fibrinogens were not different from each other. Using autoradiography the highest 58Co binding could be found in the gamma-chain with a reduced electrophoretic migration velocity, whereas B beta-and gamma-chains with unchanged electrophoretic mobility bound only small amounts. A alpha-chains of cobalt fibrinogens were apparently not loaded with 58Co. gamma-chain and alpha-chain cross-links could be observed in normal fibrins stabilized by factor XII, however, in cobalt fibrins a gamma-dimer formation was demonstrable without participation of gamma-chains with reduced electrophoretic mobility. A distinct alpha-chain cross-link could not be demonstrated either. From these and other investigations on molecular weights of both fibrinogens it was assumed that earlier observed changes of physicochemical properties and biological behaviour of cobalt fibrinogen might result from a complex binding of cobalt ions on specific structures of the fibrinogen molecule.

Amino Acid Sequence↗

Chronic mucocutaneous candidiasis with macrophage dysfunction, a plasma inhibitor, and co-existent aplastic anemia.

A 56-year-old man developed chronic mucocutaneous candidiasis (MCC) and pernicious anemia. Nine years later he developed aplastic anemia which ultimately was fatal. A small thymoma was found at autopsy. He was anergic and his mononuclear leukocytes (MNL) failed to undergo a proliferative response in culture to soluble antigens. His monocytes did not mediate a proliferative response by lymphocytes from sensitized control donors when stimulated with Monilia albicans antigen but did mediate a mixed leukocyte reaction normally. His plasma contained a poten inhibitor of -3H-thymidine incorporation by sensitized control MNL when stimulated with soluble antigens but was not inhibitory of the mixed leukocyte reaction, lymphoproliferative responses to plant mitogens, and was not shown either in vivo or in vitro to depress hematopoiesis. Patient lymphocytes were responsive to plant mitogens, Monilia antigen, in the mixed leukocyte reaction, and produced macrophage migration inhibitory factor in response to Monilia antigen. After plasmapheresis, delayed hypersensitivity and lymphoproliferative responses to soluble antigens were temporarily restored. This case implicates the macrophage in the pathogenesis of MCC and demonstrates some consequences of chronic monocyte dysfunction. The inhibitor of some expressions of cell-mediated immunity was removed by plasmapheresis.

Aged↗