Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 4 de 4
Filtrar
Más filtros










Base de datos
Intervalo de año de publicación
1.
J Dairy Sci ; 89(2): 468-82, 2006 Feb.
Artículo en Inglés | MEDLINE | ID: mdl-16428616

RESUMEN

Two sets of Cheddar cheese were made in which the milk protein level (%, wt/wt) was increased from 3.3 (Control A, CA) to 3.6 (set A) or from 3.3 (control B, CB) to 4.0 (set B) by the addition of phosphocasein (PC), milk protein concentrate (MPC), or freshly prepared ultrafiltered milk retentate (UFR). The cheeses were denoted CA, PCA, MPCA, and UFRA from set A, and CB, PCB, MPCB, and UFRB, from set B, respectively. The level of cheese moisture decreased significantly on increasing milk protein level from 3.3 to 3.6 or 4.0% (wt/wt), but was not affected significantly by the method of protein standardization. The percentage milk fat recovered to cheese increased significantly on increasing the level of milk protein from 3.3 to 3.6% (wt/wt) with PC, and from 3.3 to 4.0% (wt/wt) with PC, MPC, and UFR. Increasing milk protein level from 3.3 to 4.0% (wt/wt) with PC significantly increased the percentage of milk protein recovered to cheese. Actual cheese yield increased significantly with milk protein level. The yield of cheese per 100 kg of milk normalized to reference levels of fat (3.4%, wt/wt) and casein (2.53%, wt/wt) indicated no significant effects of protein content or standardization treatment on yield. However, the moisture-adjusted yield per 100 kg of milk with reference levels of fat and casein increased significantly on increasing the protein content from 3.3 to 3.6% (wt/wt) with MPC and from 3.3 to 4.0% (wt/wt) with PC, MPC, and UFR.


Asunto(s)
Queso/análisis , Proteínas de la Leche/análisis , Animales , Caseínas/análisis , Queso/normas , Fenómenos Químicos , Química Física , Quimosina/metabolismo , Grasas/análisis , Filtración , Manipulación de Alimentos/métodos , Modelos Lineales , Leche/química , Proteína de Suero de Leche
2.
N Y State Dent J ; 64(2): 26-31, 1998 Feb.
Artículo en Inglés | MEDLINE | ID: mdl-9542391

RESUMEN

Epilepsy is a relatively common problem in children, adults and the elderly. Dentists need to be familiar with the various manifestations of the disease, the anticonvulsant medications (AEDs) the patients are taking, and the complications and side effects of these drugs. In this article the types of seizures and AEDs in common use are described. Guidelines for treatment planning are given. Recommendations are made for managing the patient who has a seizure in the dental office.


Asunto(s)
Atención Dental para Enfermos Crónicos , Epilepsia/fisiopatología , Adulto , Anciano , Anticonvulsivantes/efectos adversos , Anticonvulsivantes/uso terapéutico , Carbamazepina/uso terapéutico , Niño , Urgencias Médicas , Epilepsias Parciales/clasificación , Epilepsias Parciales/tratamiento farmacológico , Epilepsias Parciales/etiología , Epilepsias Parciales/fisiopatología , Epilepsia/clasificación , Epilepsia/tratamiento farmacológico , Epilepsia Generalizada/clasificación , Epilepsia Generalizada/tratamiento farmacológico , Epilepsia Generalizada/etiología , Epilepsia Generalizada/fisiopatología , Epilepsia Tónico-Clónica/tratamiento farmacológico , Epilepsia Tónico-Clónica/fisiopatología , Femenino , Humanos , Responsabilidad Legal , Masculino , Anamnesis , Persona de Mediana Edad , Planificación de Atención al Paciente , Fenobarbital/uso terapéutico , Fenitoína/uso terapéutico , Ácido Valproico/uso terapéutico
3.
Biochimie ; 79(8): 503-8, 1997 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-9451451

RESUMEN

In order to extend our knowledge of factors important in the surface activity of melittin, cysteine was substituted for lysine-21 and lysine-21/glutamine-25 in a pair of synthetic peptide analogues. The first of these changes resulted in only modest effects on secondary structure (determined in 50% trifluoroethanol), emulsification and surface tension properties. Introduction of a second cysteine greatly reduced both the rate of surface tension decay and the equilibrium surface tension attained, although secondary structure (determined in 50% trifluoroethanol) was only slightly affected by this modification. This latter peptide completely lacked emulsification and haemolytic properties and was found to oligomerise readily due to the formation of intermolecular, disulphide bridges. These results indicate that oligomerisation abolishes surface activity in melittin.


Asunto(s)
Cisteína/química , Meliteno/análogos & derivados , Animales , Dicroismo Circular , Electroforesis en Gel de Poliacrilamida , Emulsiones , Hemólisis , Estructura Secundaria de Proteína , Ovinos , Relación Estructura-Actividad , Tensión Superficial
SELECCIÓN DE REFERENCIAS
DETALLE DE LA BÚSQUEDA
...