Blood pressure variability in acute ischemic stroke depends on hemispheric stroke location.

The relationship between blood pressure (BP) variability and stroke location was examined in 85 patients admitted with acute ischemic stroke. The patients were divided into three groups according to stroke location: right hemisphere (32 patients), left hemisphere (30 patients) and non-localized (23 patients). BP upon admission was 147.94/76.53 +/- 20.72/13.70 mmHg in the right hemisphere group, 151.81/76.10 +/- 25.69/16.23 mmHg in the left hemisphere and 155.23/83.41 +/- 30.45/15.74 in the non-localized group. The left hemisphere group had significantly (p < 0.01) greater variations in systolic and diastolic BP between days 2 and 3 and in systolic BP between days 3 and 4 after stroke compared with the other groups. BP in the left hemisphere group was less stable than in the other two groups. Non-localized patients without pre-existing hypertension had a significantly lower and more stable BP during the week following stroke than non-localized patients with pre-existing hypertension. Non-localized patients with pre-existing hypertension had the highest BP and showed no improvement during the week. Systolic BP tended to be higher and less stable in left hemisphere patients than in right hemisphere, whereas among non-localized ischemic stroke patients BP was higher in those who had a prior diagnosis of hypertension.

Domain structure of adrenocortical cytochrome P-450scc: localization of functionally important sites in the polypeptide chain.

Cytochrome P-450scc consists of two domains linked with a short loop of the polypeptide chain; under its hydrolysis with trypsin the domains retain their associated state due to rigid noncovalent interactions. The structural characteristics of the individual domains have been investigated. It is established that domain I containing the haem and the adrenodoxin-binding site is the N-terminal, and domain II the C-terminal moiety of the polypeptide chain of cytochrome P-450scc.

The domain structure of the cholesterol side-chain cleavage cytochrome P-450 from bovine adrenocortical mitochondria. Localization of haem group and domains in the polypeptide chain.

Cytochrome P-450scc consists of two domains linked with a short loop of the polypeptide chain; under hydrolysis by trypsin the domains retain their associated state due to rigid noncovalent interactions. A partial separation of the domains by gel-chromatography on Sephadex G-200 with retention of a haem group in domain I has been achieved after incubation of the trypsin-modified cytochrome P-450scc in 50 mM phosphate buffer (pH 7.2)/1 M NaCl/0.3% sodium cholate/0.3% Tween 80. The separation of domains I and II to individual fragments of the haemoprotein polypeptide chain has been achieved by chromatography under denaturation conditions on the activated thiopropyl-Sepharose via a selective covalent immobilization of domain II. Dissociation of a complex of domains I and II has been effectuated in the presence of 7 M guanidine. Structural characteristics of individual domains have been investigated. It is established that domain I containing a haem group is the N-terminal moiety, and domain II, the C-terminal moiety of the polypeptide chain of cytochrome P-450scc. The pathways of limited trypsinolysis of the native cytochrome P-450scc have been determined. The peptides containing cysteine residues localized on the surface of domain II and responsible for the interaction of haemoprotein with activated thiopropyl-Sepharose have been isolated in a homogeneous form and their amino-acid sequences have been assessed.

The domain structure of the cholesterol side-chain cleavage cytochrome P-450 from bovine adrenocortical mitochondria.

A homogeneous cytochrome P-450scc preparation with a specific enzyme content of 18 nmol/1 mg protein has been obtained using affinity chromatography on adrenodoxin-Sepharose under optimal conditions of the protein adsorption onto and desorption from the affinity sorbent. The data on the N-terminal amino acid sequence of the enzyme, along with the results of electrophoretic and spectrophotometric analyses favoured the multistage cholesterol transformation to pregnenolone to be catalyzed by single species of cytochrome P-450scc consisting of one polypeptide chain. Limited proteolysis of cytochrome P-450scc with trypsin resulted, at the initial stages, in the formation (in an equimolar ratio) of two large polypeptide fragments, I and II, with Mr 27000 and 22000, respectively. Prolonged action of trypsin led to the digestion of fragment II and the formation of a stoichiometric amount of fragment III, Mr of about 14000. Cytochrome P-450scc converted by trypsin into equimolar mixtures of fragments I and II or I and III retained the major spectral and functional properties of the native protein. The aspartyl-prolyl linkages, sulphhydryl groups, and surface tyrosine residues are distributed nonuniformly among fragments I and II. These data, as well as a different resistance of the fragments to the action of trypsin, suggest that cytochrome P-450scc consists of two independently folded domains linked with a short loop of the polypeptide chain, the domains being rigidly associated under neutral conditions.