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Biomedical subjects

Y S Rajput

Publications and source records attributed to Y S Rajput.

7 recordsLinked to original sources
PubMed1999

Monoclonal antibodies against bovine growth hormone.

A number of mouse x mouse hybridomas producing monoclonal antibodies (MAbs) against bovine growth hormone (bGH) were prepared by fusion of spleen cells from bGH-primed mice (Balb/c) with non-secretory mouse myeloma cells (PAIOP3) and characterized. MAbs obtained from three fusion experiments belonged to IgM, IgG1 and IgG2b class/subclass of antibodies. Cross-reaction studies indicated that generated antibodies were against three different epitopes of bGH. VIA6E8 (IgG1) and VIIB2E11C9 (IgM) did not cross-react with ovine prolactin (oPRL), ovine leutinizing hormone (oLH) and porcine follicle stimulating hormone. Antibody VIB3C9E8 (IgM) exhibited cross-reaction with oPRL and oLH. Antibody VIC1F9 (IgG2b) cross reacted with oPRL. All MAbs were against conformational epitopes of bGH.

Animals↗
PubMed1999

Immunosuppressive activity in buffalo placenta.

Immunosuppressive activity in buffalo placenta was evaluated by measuring proliferation of lymphocytes in presence of phytohaemagglutinin (PHA) alone or PHA plus placental proteins. The immunosuppressive activity was dose-dependent over the protein concentration range of 10-50 micrograms/ml. Proteins from both cotyledon and non-cotyledon portions of placenta exhibited immunosuppressive activity. Fractions obtained with 0-40, 40-60 and 60-80% saturated ammonium sulphate exhibited 70, 73 and 75% suppression, respectively. PBS-soluble placental proteins were resolved on G-100 column into three peaks that exhibited 69 (peak 1), 55 (peak 2) and 73% (peak 3) suppression. Exogenously added interleukin-1 (IL-1) failed to reverse the suppression caused by buffalo placental proteins.

Animals↗
PubMed1995

Purification and characterization of an acid phosphatase from Arachis hypogaea.

An acid phosphatase from Arachis hypogaea (peanuts) has been purified. The electrophoretically homogeneous enzyme preparation is free of any phophodiesterase activity. The enzyme has a molecular weight of 120,000. Among the various phosphomonoesters tested, p-nitrophenylphosphate was found to be its most effective substrate. The Km for p-nitrophenylphosphate was 1.21 mM at pH 5.0 and 25 degrees C. The enzyme was thermostable and did not loose activity after 1 hr at 50 degrees C.

Acid Phosphatase↗
PubMed1988

Preparation of heteroenzyme conjugates: trypsin-chymotrypsin and trypsin-alkaline phosphatase.

Hybrid enzymes which have two different enzyme activities linked together covalently may be useful reagents for various applications, such as the determination of complex biological structures. The present paper describes the preparation and purification of two such enzyme-enzyme conjugates, namely, trypsin-chymotrypsin and trypsin-alkaline phosphatase. Whereas the former has been prepared by using the well-known bifunctional reagent glutaraldehyde, the latter exploited the Schiff base formation between the oxidized carbohydrate moiety of alkaline phosphatase and the free amino groups of trypsin.

Alkaline Phosphatase↗
PubMed1980

Distribution of acid and alkaline phosphatase in buffalo spermatozoa.

The distribution of acid phosphatase (EC 3.1.3.1) and alkaline phosphatase (EC 3.1.3.2) was studied in the head, midpiece and tail fractions of buffalo spermatozoa. Fractionation was achieved by the basic principles of ultrasonication and density gradient centrifugation. The activity of acid phosphatase in the head, midpiece and tail fractions was 7.30, 11.55 and 47.10 and for alkaline phosphatase 1.74, 6.95 and 26.71 respectively; the unit being microgram of inorganic phosphorus liberated/mg of protein/h at 37 degrees C.

Acid Phosphatase↗
PubMedDate not supplied

A conjugate of trypsin and chymotrypsin.

A heteroenzyme conjugate retaining activities of two component enzymes from trypsin and chymotrypsin was prepared using N-succinimidyl pyridyl dithiopropionate as crosslinking reagent. The conjugate bound to both trypsin and chymotrypsin affinity columns. Trypsin and chymotrypsin were linked in the ratio of 1:1 on mol basis. The conjugate, when treated with dimethyladipimidate, showed decreased autolysis of its trypsin component.

Chymotrypsin↗