Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 7 de 7
Filtrar
Añadir filtros








Intervalo de año
1.
Artículo | IMSEAR | ID: sea-196032

RESUMEN

This study was undertaken to know the incidence and management practices of snakebite envenomation at the First Referral Unit - Sub-District Hospital, Dahanu, Maharashtra, India. Retrospective analysis of snakebite case records (n=145) was carried out for one-year period (January to December 2014). The annual incidence of snakebite was 36 per 100,000 population with case fatality rate of 4.5 per cent. Venomous snakebites were 76 per cent and non-venomous snakebites were 24 per cent. Overall, snakebites were more common in males (52.4%) than females (47.6%). Majority of the snakebites (66%) were in the age group of 18-45 yr. Seasonal variation was observed with highest snakebites in monsoon (58%). Lower extremities were the most common site of bites (63%). Neurotoxic and vasculotoxic envenomation were reported in 19 and 27 per cent snakebite cases, respectively. Anti-snake venom (ASV) was administered at an average dose of 7.5±0.63 vials (range 2-40, median 6). There was no uniform protocol followed for ASV administration as per the National Snakebite Management Protocol of Government of India (2009).

2.
Indian J Exp Biol ; 2013 Dec; 51(12): 1055-1062
Artículo en Inglés | IMSEAR | ID: sea-150292

RESUMEN

yielded an average particle size of 120 nm with 70% encapsulation-efficiency. In vitro release profile of NP-OP showed sustained release of OP for 21 days. In vivo anti-fertility studies were conducted in marmosets. Results indicated that control animals conceived in the same cycle while two of three treated animals failed to conceive in treatment cycle. The in vivo studies thus corroborate with in vitro release of OP, demonstrating its anti-fertility activity in 66% of animals.


Asunto(s)
Animales , Callithrix/fisiología , Proteínas Portadoras/administración & dosificación , Proteínas Portadoras/química , Anticoncepción , Femenino , Humanos , Nanopartículas/administración & dosificación , Nanopartículas/química , Folículo Ovárico/química , Tamaño de la Partícula , Fragmentos de Péptidos/administración & dosificación , Fragmentos de Péptidos/química , Polímeros/administración & dosificación , Polímeros/química
3.
Indian J Biochem Biophys ; 1992 Jun; 29(3): 277-81
Artículo en Inglés | IMSEAR | ID: sea-29006

RESUMEN

Rabbit antibodies to native riboflavin carrier protein (RCP), are to a large extent directed towards the conformational epitopes and antibodies to disulphide bond reduced carboxymethylated riboflavin carrier protein (RCM-RCP) to the sequential epitopes. Taking advantage of this premise and in order to map the epitopes of RCP recognized by the antibodies, enzyme-linked immunosorbent assays were validated for RCP and RCM-RCP using the Avidin-Biotin system. The usefulness of these assays were illustrated when antigenicity of peptides derived from RCM-RCP following trypsinization were examined. Two major (T1,T2) and one minor peptide (T3) fractions were obtained when the tryptic peptides were fractionated on DEAE-cellulose. RCP has a blocked N-terminal. Tryptic peptides (T1 and T2) on microsequencing revealed the absence of an N-terminal amino acid, indicating that these fragments emanate from the N-terminal region of RCP. In support of this observation is the finding that antipeptide antibody to cRCP (10-24) of cRCP interacted with T1 as well as T2 indicating the presence of the sequential epitope (10-24) of cRCP in these fragments. In RCP-ELISA, only T2 displaced RCP and peptides T1 and T2 displaced RCM-RCP in RCM-RCP ELISA. Differences in the ability of these fragments (T1 and T2) to displace RCP and RCM-RCP reflect the subtle changes in the spatial structures of these epitopes in RCP and RCM-RCP.


Asunto(s)
Secuencia de Aminoácidos , Animales , Proteínas Portadoras/análisis , Ensayo de Inmunoadsorción Enzimática , Epítopos/análisis , Proteínas de Transporte de Membrana , Datos de Secuencia Molecular , Fragmentos de Péptidos/inmunología , Péptidos/síntesis química , Riboflavina/metabolismo
4.
Indian J Exp Biol ; 1991 Oct; 29(10): 897-9
Artículo en Inglés | IMSEAR | ID: sea-62282

RESUMEN

A synthetic nonapeptide, which is C-terminal sequence of 94-amino acid of prostatic inhibin peptide was tested for progesterone and estrogen secretion by mouse granulosa cell cultures. Nonapeptide suppressed the progesterone and estrogen synthesis, the magnitude of suppression was highest at 5 ng dose level for progesterone and 50 ng dose level for estradiol. The study suggests that, nonapeptide exerts its effect by impairing the binding of FSH to granulosa cell receptors.


Asunto(s)
Animales , Células Cultivadas , Relación Dosis-Respuesta a Droga , Femenino , Hormona Folículo Estimulante/metabolismo , Hormonas Esteroides Gonadales/biosíntesis , Gonadotropinas Equinas , Células de la Granulosa/efectos de los fármacos , Inhibinas/farmacología , Ratones , Fragmentos de Péptidos , Progesterona/biosíntesis
5.
Indian J Exp Biol ; 1989 Jan; 27(1): 10-3
Artículo en Inglés | IMSEAR | ID: sea-59494

RESUMEN

Synthesis and biological profile of a decapeptide analogue, [Tyr85, Cys(Acm)87]85-94 of human seminal plasma inhibin (HSPI) are described. The peptide suppressed the circulatory levels of follicle stimulating hormone (FSH) in adult male rats. No change in the levels of luteinizing hormone (LH) and prolactin (Prl) was observed. Whereas the peptide suppressed the release of both FSH and LH in vitro. This decapeptide is the smallest peptide reported so far to have FSH suppressing activity.


Asunto(s)
Animales , Cromatografía Líquida de Alta Presión , Hormona Folículo Estimulante/metabolismo , Inhibinas/análogos & derivados , Hormona Luteinizante/metabolismo , Masculino , Fragmentos de Péptidos , Prolactina/metabolismo , Proteínas de Secreción Prostática , Proteínas/farmacología , Ratas , Proteínas de Plasma Seminal
SELECCIÓN DE REFERENCIAS
DETALLE DE LA BÚSQUEDA