Biomedical subjects
H Franz
Publications and source records attributed to H Franz.
[Pain control in otorhinolaryngologic treatment using Dolo-Buscopan].
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[Course, cause and action of epidermis migration of the tympanic membrane].
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[On the indirect detection of non-lipid substances with sudan black B].
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[Panthenol as antagonist of muscle relaxants].
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The training of a nursing staff in psychosomatic medicine in a medical clinic.
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Identification of the normal microglial population in human and rodent nervous tissue using lectin-histochemistry.
Mistletoe lectin-1 (ML-1) and Ricinus communis agglutinin-120 (RCA-1) both possess D-galactose-specific surface-binding sites. They were used to selectively identify microglial populations in aldehyde-fixed normal brain tissue by lectin immunohistochemistry on paraffin and frozen sections. Mistletoe lectin-1 was superior to RCA-1 in labelling microglia in the rat brain, whereas RCA-1 labelled human microglia better than ML-1. Thus, RCA-1 and ML-1 supplement each other for identifying microglial in human and rodent central nervous system tissues. The high reproducibility of the results and the applicability of the technique to routine histology, using formalin-fixed tissue, should facilitate study of the histogenesis and role of microglia in the CNS.
[Diseases caused by atypical mycobacteria--diagnosis and therapy].
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[The structure of toxic protein, the mistletoe lectin, at different pH: the study using intrinsic fluorescence method].
The effects of pH on the conformation of mistletoe lectin I and its isolated A- and B-subunits has been investigated by using the methods of intrinsic fluorescence. By the denaturating action of guanidine hydrochloride and the influence of the quenchers (I-, Cs+, acrylamide) the structural stability of the native protein and its isolated subunits was estimated. Treatment of the protein with the denaturant and quenchers revealed its different structure at pH 7.0 and 4.0. At pH 4.0 tryptophan residues become more accessible to quenchers, positive charge of the surrounding area increases and the protein becomes more stable to the action of denaturant. The structure of the isolated A- and B-chains of mistletoe lectin I differs considerably from that of the whole protein: a) its stability to the action of guanidine hydrochloride is lower; b) it depends on the ionic strength of the solvent; c) it is characterized by increased accessibility of tryptophan residues to quenchers (for B-chain). Differences between the conformations of the isolated chains at pH 7.0 and 4.0 are marked more strongly; moreover, at pH 4.5 the B-chain undergoes structural transition. The possible relationship between structural peculiarities of mistletoe lectin I and the mechanism of its transmembrane transfer is discussed.
[Results of psychological tests in females with dysmenorrhea].
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Preparation of antibody-lectin conjugate using reversibly inactivated concanavalin A.
We have tried to modify the lectin-immunotest first described by Guesdon and Avrameas by use of inactivated ConA for the preparation of the conjugates. The inactivation of ConA took place by removal of the bivalent cations Mn++ and Ca++ by means of dialysis against oxalic acid at pH 4.0. The inactivated ConA was coupled to an anti-rabbit IgG antibody using glutaraldehyde. Following the antigen-antibody reaction the lectin could be reactivated. The Con A was again able to react with horseradish peroxidase. The reactivation and the binding of the enzyme can be performed as a one-step procedure. In comparison to the conjugate of the same antibody and active ConA the conjugate of inactivated ConA showed the same sensitivity in the determination of the corresponding antigen but the concentration of the antibody in the working dilution had to be increased.