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H M Gupta

Publications and source records attributed to H M Gupta.

8 recordsLinked to original sources

Purification and partial characterization of an induced antibacterial protein in the silkworm, Bombyx mori.

Injection of live Escherichia coli into larvae of the silkworm, Bombyx mori, induces antibacterial activity in the hemolymph. The major induced antibacterial activity was purified in two steps by CM-Sephadex C-50 and Sephadex G-100 column chromatography. After trypsin treatment, the purified antibacterial protein lost its activity and the antibacterial activity was found to be partially heat labile. The purified protein was a single polypeptide chain of molecular weight 16 kDa. The 20 N-terminal amino acid sequence of the protein was determined and this sequence showed homology with the N-terminal amino acid sequence of lysozymes reported in other species. The purified protein was found to have comparable antibacterial activity against both E. coli and Micrococcus luteus. The purification of antibacterial protein and the antibacterial properties of the purified protein are discussed.

Amino Acid Sequence↗

A novel computer modeling approach to the structures of small bioactive peptides: the structure of gonadotropin releasing hormone.

A novel computer modeling approach suitable for the structure analysis of small bioactive peptides has been developed. This approach involves identification of conformational patterns in protein structure data bank based on the sequence homology with the bioactive peptide. The models built on the basis of this homology and having common conformational patterns are analyzed under the structural constraints derived from the activity data of various synthetic analogs of the peptide. Application of this procedure to the gonadotropin-releasing hormone (GnRH) resulted in a library of possible structures for GnRH, 9 among which shared a common beta-turn. Further analysis of the structures containing the beta-turn motif, in the context of the structure-activity data, led to a model for the active conformation of GnRH. The topology of the putative receptor binding site of the hormone is defined by a contiguous surface formed through an appropriate juxtaposition of the N-terminal pGlu1, the guanidyl group of Arg8, aromatic side chain of Trp3, and the Gly10-NH2 at the C-terminal end.

Amino Acid Sequence↗

Hyporesponsiveness to a GnRH vaccine in a non-responder mouse strain is T-cell mediated.

Immunization of rats and monkeys with the decapeptide gonadotropin releasing hormone (GnRH) linked to carriers such as diphtheria toxoid (DT) or tetanus toxoid (TT) results in a marked atrophy of the prostate. This vaccine is now being explored for its potential in the "immunosurgery" of prostatic hypertrophy in men and is currently undergoing Phase I/II clinical trials. We have been investigating immunogenetic aspects of immune responses to this hapten-carrier conjugate, and in a recent communication we described the responses of different strains of mice to GnRH conjugated to DT (GnRH-DT). Mice of the 129 (H-2b) strain were found to be non-responders to GnRH. However, further immunization of GnRH-DT-immunized 129 mice with GnRH linked to an alternate carrier, TT, resulted in the production of high levels of anti-GnRH antibodies. This showed that 129 mice are not deficient in GnRH-specific B cells and that the lack of response to GnRH in 129 mice is possibly due to (i) the lack of appropriate helper T-cells or (ii) the presence of suppressor cells. In this report we present evidence to support the existence of suppressor cells in GnRH-DT-immunized 129 mice.

Animals↗

Carrier-induced suppression of the antibody response to a 'self' hapten.

Immunization of male rats and monkeys with gonadotropin-releasing hormone (GnRH) conjugated to a carrier results in a dramatic atrophy of the prostate. GnRH, linked to either diphtheria toxoid or tetanus toxoid as carrier, is now being evaluated for its use in the immunotherapy of hormone-dependent prostate enlargement in men. This report deals with the phenomenon of carrier-induced, epitope-specific regulation in the GnRH-carrier system. In experiments designed to assess the influence of the carrier on antibody responses to the 'self' hapten GnRH, we show that preimmunization with carriers diphtheria toxoid and tetanus toxoid results in a strain-dependent inhibition of anti-GnRH responses in mice. Results of adoptive transfer experiments indicate that T cells from carrier-presensitized mice are responsible for suppression of anti-haptenic antibodies and that T cells from conjugate-immunized mice, on the other hand, can actually help overcome hyporesponsiveness.

Animals↗