C to T and/or G to A transitions are responsible for loss of a MspI restriction site at the 5′-end of the human apolipoprotein AI gene

We detected the loss of a MspI restriction site by a C to T transition at +83 bp and a G to A transition at +84 bp of the 5-end non-coding region of the human apolipoprotein AI gene. This base change occurred at the hot spot (CCGG) for methylation, which may be important in the regulation of gene expression. The population frequency for the loss of the MspI site is 6.1%.     

鄂西南山地植被的基本特征

本文系湖北省区划办委托进行的湖北植被类型图、植被区划图过程中的一个阶段性小结。鄂西南山地位于中国亚热带东部(湿润)常绿阔叶林亚区域,为湖北植被区划中鄂西南山地植被区,所属范围包括整个鄂西自治州、宜昌地区的大部及神农架南坡。约当北纬29°05′—31°22′,东经108°30′—111°47′的地理位置。     

SAR in rats exposed in 2,450-MHz circularly polarized waveguides

Average specific absorption rates (SARs) for live rats exposed in 2,450-MHz circularly polarized waveguides were estimated from the total system loss determined from measurements using five power meters, and a correction factor representing actual SAR/apparent SAR. The actual SAR was measured by twin-well calorimetry and the apparent SAR by power meters. Values were obtained for carcasses of various body masses for five orientations. The average SAR with free movement in the cages changed less than threefold as the rats grew from 200 to 700 g. The ratio of peak to average SAR in the body was less than 3. These results indicate relatively constant energy disposition in rats exposed in the circularly polarized waveguide.     

Modifications of myelin basic protein which occur during its isolation.

Abstract— Chromatography of myelin basic protein (BP) on carboxymethylcellulose gives a pattern of multiple components, of which three are major. Component 1 is considered the unmodified species of BP while component 2 has been found to be modified primarily by deamidation and component 3 by phosphorylation (Chou et al., 1976). ³ 3 The numbering system for the components is that used by DEIBLER & MARTENSON (1973) for guinea pig BP and is preferred over the reverse system of numbering used by CHOU et al. (1976); i.e. components 1, 2 and 3 of DEIBLER & MARTENSON (1973) are the same as components 6, 5 and 4 of CHOU et al. (1976), respectively.
In contrast to BP prepared from tissue delipidated in the standard fashion in chloroform–methanol (CM powder), BP prepared from tissue delipidated first in acetone and then in chloroform–methanol (ACM powder) gave an elution pattern on carboxymethylcellulose characterized by a decrease in component 1 and an increase in the earlier eluting, less basic components. Studies with radiolabelled component 1 showed that this difference in elution patterns was due to the partial conversion of component 1 to less basic components during the extraction of ACM powder at neutral pH. The components derived from component 1 (D2, D3 and D4) were then isolated and subjected to tryptic peptide map analyses and determination of their carboxy-terminal arginine content and content of phosphorus. None of the derived components contained phosphorus but tryptic peptide map analyses did show the presence of two minor peptides, T14M₂ and T20M, previously found in component 2 from CM powder and considered to be the deamidation products of their parent peptides T14 and T20 (Chou et al., 1976). In addition components D3 and D4 were shown to have lost appreciable arginine from their carboxy-termini. Since none of the efforts to reduce enzyme activity in vitro had any appreciable effect on components 2 and 3 it was concluded that phosphorylation probably occurs exclusively in vivo, that deamidation occurs both in vivo and in vitro and that loss of carboxy-terminal arginine occurs exclusively in vitro.     

Functional groups at the catalytic site of F1 adenosine triphosphatase

The protection of F1 ATPase by inorganic phosphate, ADP, ATP, and magnesium ion against inactivation by 1-fluoro-2,4-dinitrobenzene, 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole, and 1-(ethoxycarbonyl)-2-ethoxy-1,2-dihydroquinoline, respectively, has been investigated. Dissociation equilibrium constants and rate constants for the labeling reactions have been deduced from a quantitative treatment of the kinetic data. Comparison of these dissociation constants with each other and with the corresponding literature values indicates that the essential Tyr, Arg, Lys, and Glu or Asp residues are indeed located at the catalytic site of the enzyme. Examination of the rate constants for the labeling reactions in the presence of excess inorganic phosphate, ADP, ATP, or magnesium ion, respectively, suggests that the essential phenol and amino groups are located nearer to the bound inorganic phosphate or the gamma-phosphate group than to the alpha- or beta-phosphate group of the bound ATP, that the essential guanidinium group is located nearer to the alpha- or beta-phosphate group than to the gamma-phosphate group of the bound ATP or the bound inorganic phosphate, and that the essential carboxylate group is located slightly farther away but complexed with magnesium ion which it shares with the bound inorganic phosphate. A mechanism consistent with these topographical relationships is proposed for the catalytic hydrolysis and synthesis of ATP.     

Crystal structure of cholestanyl caprylate and binary phase behavior with cholesteryl caprylate

The crystal structure of cholestanyl n-octanoate (caprylate) (C35H62O2) is monoclinic with space group A2 and cell dimensions a = 10.103(7), b = 7.646(7), c = 87.63(7) A, beta = 90.51(6) degrees; Z = 8 [two molecules (A, B) in asymmetric unit], V = 6769 A3, Dc = 1.010 g cm-3. Integrated X-ray intensities for 3798 reflections with I greater than 2 sigma (I) were measured with a rotating anode diffractometer at room temperature. The structure was determined using direct methods. Block diagonal least squares refinement gave R = 0.111. Molecules A and B have almost fully extended conformations, but differ significantly in the rotation about the ester bond and in the C17 chains. The molecular packing in the crystal structure of cholestanyl caprylate consists of stacked bilayers each having d002 = 43.8 A in thickness and within each bilayer, cholestanols pack with cholestanols and caprylate chains pack with caprylate chains. The crystal structure is very similar to that of cholesteryl myristate but is quite different from that of cholesteryl caprylate. The phase equilibria of the cholestanyl caprylate/cholesteryl caprylate binary system have been shown to involve limited mutual solubility of the two components and to have a eutectic point at 73% cholestanyl caprylate. The cholesteric mesophase is monotropic at all compositions except for a narrow range near the eutectic point where it is enantiotropic.     

The biology of beta-adrenergic receptors: analysis in human epidermoid carcinoma A431 cells.

1. G-protein-linked transmembrane signaling has emerged as a major pathway for information transduction across the cell membrane. 2. In addition to photopigments that propagate the signal from light, cell-surface receptors for hormones, neurotransmitters, and autacoids propagate signals from ligand binding to membrane-bound effector units via G-proteins. 3. Biochemical and molecular features of one prominent member of these receptors, the beta-adrenergic receptor, will be highlighted in the present article. 4. The role of the human epidermoid carcinoma A431 cells as a model for the study of the structure and biology of beta-adrenergic receptors will be emphasized. 5. A model for receptor regulation, gleaned from recent advances in the biochemistry, cell and molecular biology of beta-adrenergic receptors, is discussed.