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1.
Biofizika ; 52(5): 780-4, 2007.
Artigo em Russo | MEDLINE | ID: mdl-17969908

RESUMO

The influence of sugars (glucose, fructose, and sucrose) on the hydration characteristics of serum albumin was studied using 1H NMR spectroscopy in combination with layer-by-layer freezing-out of bulk and interfacial water. It was found that the presence of sugars in protein solution leads to a considerable decrease in the concentration of bound water at T < 273 K; i. e., sugars cause the dehydration of protein molecules, which may be caused by those alterations in albumin structure that are associated with the formation of more compact globular structures. The most considerable effect was recorded in case of sucrose, which causes a decrease in the dehydration of albumin by at least one order of magnitude. The interfacial energy values for the protein/water system were calculated.


Assuntos
Frutose/química , Glucose/química , Soroalbumina Bovina/química , Sacarose/química , Animais , Bovinos , Temperatura Baixa , Humanos , Ressonância Magnética Nuclear Biomolecular
2.
Biofizika ; 42(5): 1040-6, 1997.
Artigo em Russo | MEDLINE | ID: mdl-9410031

RESUMO

The experimental technique is presented which allows the investigation of water at the adsorbent-biopolymer interface by record of temperature dependencies of 1H NMR signals during the heating of previously frozen water suspensions. It was found that the adsorption of protein conconovalin A resulted in twofold decrease of strong bound water amount and in 70% increase of loosely bound one. The mean-value of Gibbs energy decreased twice for strong bound water and increased twice for loosely bound one. The external layer of hydrate shell of silica particles with adsorbed conconovalin A was organized by protein molecules. This conclusion is based on the observed total increase of loosely bound water amount, as a result, of protein adsorption, although its amount with respect to a protein molecule decreased.


Assuntos
Concanavalina A/química , Dióxido de Silício/química , Água/química , Adsorção , Congelamento , Ressonância Magnética Nuclear Biomolecular , Prótons , Propriedades de Superfície , Suspensões , Termodinâmica
3.
Ukr Biokhim Zh (1978) ; 64(4): 112-6, 1992.
Artigo em Russo | MEDLINE | ID: mdl-1333107

RESUMO

The binding of hydroxylated disperse silica (I) surface and surface, modified by glycerol (II), with components of above-membrane matrix of bovine reproductive cell and seminal plasma was investigated. It was found that structure of inorganic support defined the character of binding SiO2 with proteins and glycoproteins, including those with hexose and N-acetylneuraminic acid as terminal residue. Value of binding depends on concentration of disperse silica contacting with biomaterial.


Assuntos
Membrana Celular/química , Glicerol/química , Sêmen/química , Dióxido de Silício , Espermatozoides/química , Adsorção , Animais , Bovinos , Glicoproteínas/química , Masculino , Proteínas/química
4.
Ukr Biokhim Zh (1978) ; 64(3): 106-10, 1992.
Artigo em Russo | MEDLINE | ID: mdl-1332236

RESUMO

The interaction of various disperse silica of I, II, III kind possessing various structure of surface groups (-OH; -O-CH2-CH2-O-CH2-CH2OH; -O-CH2-CH2-NH2 respectively) was investigated with some above membrane matrix polymers of bovine reproductive cells and seminal plasma (namely the surface proteins and carbohydrate polymers containing the N-acetyl-neuraminic acid (NANA) as terminal residue). Protein binding was preferentially observed for silica surface modified by aminoethoxy--and ethylene glycol groups and depended on concentration of silica in the mixture. It was found that biopolymers containing carbohydrate groups had larger affinity to I than to II or III. The binding value of I-III was 12-16% with respect to plasma proteins. Silicas I and II with -OH-groups on the surface absorb 17-21% N-ANA-containing polymers of bovine seminal plasma.


Assuntos
Sêmen/química , Dióxido de Silício/química , Espermatozoides/química , Animais , Biopolímeros , Carboidratos/química , Bovinos , Masculino , Ligação Proteica , Propriedades de Superfície
5.
Ukr Biokhim Zh (1978) ; 60(5): 67-71, 1988.
Artigo em Russo | MEDLINE | ID: mdl-2849828

RESUMO

The nature of contact interactions of highly disperse silica with the surface of bovine reproductive cells and seminal plasma is investigated. Surface proteins and glycoproteids, containing N-acetylneuraminic acid as a terminal residue, are shown to participate in this process. It is found that the efficiency of contact interaction falls with an increase in the concentration of the disperse silica from 0.1% to 1%.


Assuntos
Glândulas Seminais/metabolismo , Dióxido de Silício , Espermatozoides/metabolismo , Animais , Líquidos Corporais/metabolismo , Bovinos , Masculino , Glicoproteínas de Membrana/metabolismo , Contagem de Espermatozoides
6.
Ukr Biokhim Zh ; 47(2): 169-71, 1975.
Artigo em Ucraniano | MEDLINE | ID: mdl-1209758

RESUMO

The activity of reconstructed glyceraldehyde phosphate dehydrogenase and lactate dehydrogenase reactions was studied as affected by immunoglobulin G of blood serum from patients with cancer and protein positively reacting in sedimentation test for cancer which is one of its subfractions. Addition of the protein under study to the sample is shown to inhibit the glyceraldehyde phosphate dehydrogenase reaction but activates the lactate dehydrogenase one. On the basis of the data obtained a conclusion is made that the effect of immunoglobulins G in the glycolytic systems is connected with the reactions of hydrogen transfer.


Assuntos
Glicólise/efeitos dos fármacos , Imunoglobulina G , Neoplasias/imunologia , Ativação Enzimática/efeitos dos fármacos , Gliceraldeído-3-Fosfato Desidrogenases/antagonistas & inibidores , Humanos , L-Lactato Desidrogenase/metabolismo
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