среда, 10 декабря 2008 г.

The majority of the substrates

The majority of the substrates possessing enzymatic activity, exists either in fosfo - or in which interconversion from active in an inactive condition occurs as a result of the compounded action and . , including a tsamf-dependent buy cipro medicine protein kinase, transfer g-phosphatic group with on albuminous substrates, whereas hydrolysis , splitting off from them phosphatic groups. This cycle is considered a fosforilirovanie-dephosphorylization now everywhere widespread mechanism of regulation of a metabolism, and not only to enzymes, but also to to reactions, membranous and to nuclear processes. At functional level such effects are shown by physiological processes of muscular reduction, secretion and activity of neurones. Opening Greengard of that fact, that all animal cells contain a tsamf-dependent protein kinase, has led to concept creation according to which various effects are realised through this unique class of enzymes [39]. From this point of view, specificity mediated reactions is defined by character of a protein kinase and especially character of the albuminous substrates which are present at cells of given type. It is considered, that each albuminous substrate supervises the specific metabolic or physiological process which rate is enlarged or decreases at the squirrel.
The way with which help the squirrel mediates biological effects of hormones and the transmitters operating through , is presented on 4-12. Followed believe, that for a catalysis separate albuminous substrates at numerous effects there should be a set of protein kinases. However in animal cells the small number of the basic forms of this enzyme is identified only; therefore specificity of each reaction should be defined by localisation and character of albuminous substrate. Protein kinases widely differ on the dependence or buy rimonabant online independence of cyclic nucleotides (tab. 4-2). The protein kinases not dependent on cyclic nucleotides, are present at all areas of a cell and are regulated, apparently, by other intracellular signals. Recently found out class of protein kinases for the activity demands presence of lipide components of a membrane and calcium; enzymes of this class can be a part of the transmembrane supervising systems regulated by calcium. The majority of protein kinases of cells-targets supervised by hormones depends from or (less often) on a cGMP. Such protein kinases dependent on cyclic nucleotides are concentrated in cytoashes, on meet also in plasmatic membranes and in other cellular organellas. They are activated by micromolar concentration of cyclic purine nucleotides ( and a cGMP) and quickly stimulated at rising of production of cyclic nucleotides as a result of hormone action on a cellular membrane. Both types of protein kinases dependent on cyclic nucleotides are activated at nucleotide linkage by a special site of enzyme. The tsamf-dependent protein kinase in the inactive form represents , consisting of two types: for linkage and for a catalysis of carrying over of Natrii phosphas. Inactive consists of two binding, or (), and two fermental, or catalytic (), . At linkage with 2- 22 dissociates, liberating active catalytic , possessing activity [38]. It is possible to present this reaction as follows: After the formation free K-subedinitsa finds out functional similarity to tsamf-independent protein kinases, but it can be distinguished on the characteristic size (molecular mass 38000) and reactions on thermostable fiber which blocks its catalytic activity and prevents a recombination with . Catalytic , most likely, are uniform in all forms of tsamf-dependent protein kinases whereas find out specific features. It is considered, that , protein kinases liberated at dissociation, remain in the form of 2- and later are exposed to repeated association with free catalytic therefore it is restored inactive . In absence and catalytic are bound with each other to high affinity and at physiological conditions are present mainly in the form of inactive [40]. Protein kinase cGMPs-dependent have been found out in the beginning at , but after them have found and in tissues of mammals where they function otherwise, than tsamf-dependent enzyme. Their affinity to much more low, than to a cGMP, and enzymatic activity usually also concedes that of tsamf-dependent enzyme. Activation is carried out by cGMP linkage by an enzyme site, and consider, that like a tsamf-dependent protein kinase this enzyme also dissociates with liberation of active catalytic unit. Recently it has been established between two forms of enzymes dependent on cyclic nucleotides that has led to thought on their general evolutionary parentage from primitive

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