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Biomedical subjects

C F Lange

Publications and source records attributed to C F Lange.

At least 37 records · Page 2Linked to original sources
PubMed1983

"Nonfibrillar" chitin associated with walls and septa of Trichophyton mentagrophytes arthrospores.

Two morphologically distinct forms of chitin were found in the arthrospore walls and septa of Trichophyton mentagrophytes. Two-thirds of the total wall chitin was the microfibrillar and chitinase-sensitive form. The remaining chitin existed in a previously uncharacterized "nonfibrillar" form and was insensitive to the action of Streptomyces chitinase. Exhaustive digestion of the arthrospore walls and septa with beta (1 leads to 3)-glucanase and chitinase followed by extraction with NaOH (1 N, 100 degrees C, 3 h) resulted in a fraction which retained the original wall shape. This fraction consisted of 85% N-acetylglucosamine, 2.0% galactosamine, 2.5% glucose, and 0.4% amino acids, 74% of which were lysine. Both its infrared spectrum and its X-ray diffraction pattern were almost identical to those of authentic chitin. There was no evidence of the presence of muramic acid, hexuronic acid, phosphate, or sulfate in this fraction. Its resistance to chitinase was due neither to the presence of protective wall layers or melanin nor to its close or covalent association with beta-glucan. Aside from its nonfibrillarity, this hexosamine polymer differed from authentic chitin in that it was soluble in 6 N HCl and 7.5 N NaOH. The development of this nonfibrillar chitin layer in the cell wall during arthrosporogenesis of T. mentagrophytes may be related to the arthrospores being resistant to a variety of antifungal agents.

Amino Acids↗
PubMed1981

Antistreptococcal cell membrane antisera and the antigenicity of glomerular basement membrane.

Antigenic cross-reactivity between mouse or human glomerular basement membrane (GBM) and group A type 12 beta-hemolytic streptococcal cell membranes (SCM) was evaluated by immunofluorescent techniques. Neonatal tissue proved to be more reactive than adult tissue with anti-SCM and anti-GBM antisera whose specificity was toward protein epitopes. Removal of carbohydrate moieties by enzymes (CHOase), converted adult tissue antigenicity to that of the neonate. Partial removal of some CHO, especially sialic acid, gave a partial enhancement of antigenicity. Contrariwise, antisera directed toward CHO epitopes while showing some reactivity in adult tissue gave variable results in the neonatal or young tissue. Anti-CHO sera of SCM were negative while anti-CHO sera of GBM immunogens did react slightly. None of the antisera used in these studies gave positive reactivity to heart, lung or liver tissue from any mice.

Adult↗
PubMed1980

The role of glycoprotein carbohydrate in the immunological reactivity of antistreptococcal cell-membrane and antiglomerular basement-membrane antisera.

Rabbit antisera to "carbohydrate-rich" antigens prepared from group-A, type-12 streptococcal cell-membrane and human glomerular basement-membrane were found to react by an indirect fluorescent-antibody test with the glomerular basement membrane of adult human kidney. This activity was absent or diminished in neonatal tissue. Removal of the carbohydrate epitopes from the adult tissue by means of carbohydrases removed the immunological activity. Antisera against the "carbohydrate-rich" antigens showed immunological reactivities distinctly different from those against the parent native immunogens--streptococcal cell membrane or glomerular basement membrane--which proved to be directed towards the portein epitopes.

Antigen-Antibody Reactions↗
PubMed1980

Glomerular basement membrane: its antigenicity evaluated by antistreptococcal cell membrane antisera.

Rabbit antistreptococcal membrane antisera have been demonstrated to cross-react with both human and mouse glomerular basement membrane (GBM). Though some antisera may display broad antimammalian tissue, specificity select sera were found that were specific for the GBM. The antigenicity of the GBM was also shown to change with age where certain antisera reacted with adult tissue but not with young and vice versa. Two key periods were demonstrated, one starting at about 10 days and another at about 3 months. One in vitro, indirect fluorescent antibody testing the young tissue (10-20 days) was often more reactive than older tissue. By in vivo testing these same antisera showed greater activity in animals older than 3 months. These results establish that these antisera may serve as a vital adjunct to all antisera for recognition of specific GBM antigens.

Adult↗
PubMed1978

Behcet syndrome: with immunologic evaluation.

A case of Behcet syndrome with immunologic evaluation, including screening of a vulvar ulcer for IgG, IgM, IgA, and fibrinogen by direct fluorescent microscopy is presented. Attempts were made to demonstrate cellular and humoral immune responses to mucosal antigens by lymphoblast transformation in the presence of cadaver esophageal mucosal extracts and indirect immunofluorescence using autologous serum and mucosal tissue. Serial measurements of percentages of total T, active T, and B lymphocyte populations, and lymphocyte response to phytohemagglutinin (PHA) stimulation during the course of Behcet syndrome are also presented. Clinical evaluation, histology of a Behcet vulvar ulcer, and a 2-year followup with good response to chlorambucil are reviewed.

Adult↗
PubMed1977

T and B cells in pregnancy.

The present study reports on the relative percents and absolute numbers of peripheral blood total T, active T, and B lymphocytes in pregnant women throughout gestation. These data agree with other studies reporting normal T and B cell populations during pregnancy.

Adult↗
PubMed1976

Characterization of group A streptococcal M-proteins purified by two methods.

Ten different group A streptococcal M-protein preparations purified by trichloroacetic acid precipitation and three M-protein preparations purified by cellulose chromatography were examined by SDS and polyacrylamide gel electrophoresis, and analyzed for amino acid composition and N-terminal amino acids. Fingerprinting (both tryptic and chymotryptic) was performed on the cellulose purified preparations of M1, M12, and M29 proteins which showed these proteins to be structurally related. Trypsin produced mas with 37 to 42 peptides, whereas chymotrypsin digestion resulted in 8 to 12 peptides, depending on the M-type. Sequencing was performed on the M12 protein and tentative identification of nine N-terminal amino acids made. Molecular weights of the cellulose and TCA-purified M-proteins were determined by SDS gel electrophoresis and chromatography on G-200 Sephadex, with comparable results, indicating followed the patterns established for M-proteins, with high concentrations of lysine, aspartic acid, glutamic acid, alanine, and leucine. All 10 proteins had L-alanine as their N-terminal amino acid. Evidence for a one way cross-reaction between type 1 and type 29 streptococci was also found.

Amino Acid Sequence↗
PubMed1975

Increased immunologic reactivity between human glomerular basement membrane and group A type 12 streptococcal cell membrane after carbohydrase treatment.

Anti-streptococcal cell membrane and anti-human glomerular antisera were evaluated on normal human kidney sections by an indirect immunofluorescent test both before and after absorptions with homologous and heterologous membrane preparations. The observed cross-reactions were potentiated by removal of carbohydrate units from both membrane-types by carbohydrase, a mixture of carbohydrate-cleaving enzymes.

Animals↗
PubMed1975

HL-A histocompatibility antigens and their relation to disease.

Table 14 summarizes the data presented in this review. The table lists the various diseases, along with whatever HL-A-antigen associations may be present, and the ranking that is based on the accumulated confidence of the associations; also, it lists the individual antigens and those disease states in which the incidence of the various antigens is increased ro decreased. The Table should expand rapidly in future years. There are a number of problems involved in this area of research: (1) There is a scarcity and lack of stability of good reagents, as well as the general difficulty of HL-A serology. (2) Many studies are retrospective on cells that may be abnormal. We have mentioned the changing sensitivity of lymphocytes to HL-A antibodies in disease. Increased sensitivity of weak antibodies present in the HL-A antisera may create the false impression of increased frequencies. (3) What control population one selects is also of the utmost importance. One method of internal control is to include in the controls related and unrelated individuals, all tests being run at the same time, employing the same reagents, and being run by the same technician. (4) In some disease states, notably Hodgkin's disease and SLE, autoantibodies present may interfere with the HL-A antisera reactions. All of this is compounded by the fact that the lymphocyte is constantly and rapidly shedding and replacing the HL-A antigens; the rate of turnover may change in patients, thus introducing an additional problem. Finally, there is a need for a standardization of statistical tools and for the reporting of both positive and negative results [133]. The concern for a significant quantity of test data and the problems of evaluating statistical data bring out many views. Boswell, in The Life of Samuel Johnson, noted: "I recollect nothing passed this day except Johnson's quickness, who, when Dr. Beattie observed, as something remarkable which happened to him, that he had chanced to see both No. 1 and No. 1000 of the hackney-coaches. The first and the last, 'Why Sir' (said Johnson) 'there is an equal chance for one's seeing those two numbers as any other two.'" A partial solution to these problems may be offered by the evaluation of the LD antigens [49, 63, 64]. In any event, HL-A typing offers an unique opportunity for the grouping of related diseases, as similar clinical findings with related distributions of HL-A antigens may indicate disease relationships not previously considered [27].

Animals↗
PubMed1974

Simplified method for the purification of group A streptococcal M-proteins: solution of the multiple banding problem.

A simple and rapid procedure for the isolation in high yield (about a 30% recovery based on the total 30 to 60% ammonium sulfate recovery) of homogeneous purified group A streptococcal M-protein is described. M-proteins extracted from whole cells of group A streptococci by treatment with hot HCl were neutralized, fractionated with ammonium sulfate, dialyzed, lyophilized, and then subjected to treatment with hot 60% trichloroacetic acid. This was shown to produce an M-protein preparation, free of group A carbohydrate activity and extraneous antigens, in yields up to 10-fold higher than previous methods in about one-fifth the time. These M-protein preparations were shown to: (i) have similar amino acid compositions to their respective type-specific proteins purified by diethylaminoethyl and O-(carboxymethyl) cellulose chromatography, (ii) react with their respective type-specific antisera in Ouchterlony diffusion, (iii) produce antisera in rabbits capable of promoting streptococcal long-chain formation in vitro, and (iv) give only one major band on polyacrylamide gel disk electrophoresis. The data allow for an explanation of the hitherto described multiple banding M-proteins seen on acrylamide electrophoresis.

Amino Acids↗