The Thyrotropic Cell in the Atlantic Salmon,Salmo salar

The thyrotropin (TSH) producing cells are distributed in the rostral and proximal pars distalis. This cell type is the smallest and most infrequent cell of the adenohypophysis. Its cytology is similar to the smallest gonadotropic (GTH) cells although the two cell types can be separated by the size of the small secretory granules (diameter less than 200 nm) in the TSH cells. In presmolts and smolts the cells are more numerous than in parr and adult salmon and have cytological features indicating an increased activity. This was also the case after intraperitoneal injections of synthetic TRH. Antisera to carp GTH and salmon GTH cross-reacted with both the GTH and the TSH cells. Anti-human TSH cross-reacted only with the TSH cells which confirms the assumption of antigenic similarity between human and fish TSH.     

Solubilization and spectral characteristics of chlorophyll-protein complexes isolated from the thermophilic blue-green alga Synechococcus lividus

The thermophilic blue-green alga Synechococcus lividus was grown at 38 and 55°C. The reaction center chlorophyll-protein complexes (CP) of Photosystem (PS I) and PS II, CP a_I and CP a_II, were isolated by sodium dodecyl sulphate (SDS) polyacrylamide gel electrophoresis at 4°C. SDS solubilization of thylakoids was performed in the temperature range 0–65°C. The low-temperature absorption and fluorescence emission spectral properties of the isolated chlorophyll-protein complexes were analyzed. Only traces of CP a_I were solubilized at temperatures below the lipid phase transition temperature. Instead, a minor PS I component, CP a′_I, was obtained that had absorption and fluorescence characteristics similar to those of CP a_I. CP a′_I had a slightly lower mobility than CP a_I in SDS-polyacrylamide gel electrophoresis. The amount of CP a_I in the gel scan profile increased dramatically when solubilization was carried out above the phase transition temperatures, but started to decrease above 60°C. CP a_II, on the other hand, could be efficiently extracted even at 0°C and was stable in the scan profile up to extraction temperatures of 30–40°C. Low-temperature absorption and fluorescence emission spectra were typical for CP a_I and CP a_II and no specific effects of the two growth temperatures on these properties were observed. The phase transition temperature was considered to be critical for the solubilization of CP a_I, either because of the difficulties of SDS (especially as it forms micelles at low temperatures) in penetrating the solidified membrane lipids at temperatures below that of the phase transition or because the CP a_I monomers of the PS I antennae are so strongly bound to each other that they cannot be dissociated by SDS before thermal agitation has reached a certain level that is achieved above the phase transition temperature. We consider both the difficulties in solubilizing CP a_I at sub-transition temperatures and the heat stability of the two complexes as adaptations which enable Synechococcus to grow under extreme high-temperature regimes.     

Fractionation of Soluble Copper- and Zinc-Binding Proteins From Cattle Liver

The distribution of copper and zinc among soluble proteins in liver from normal slaughter cattle was examined after gel filtration of the proteins. Gopper- and zinc-binding proteins were mainly separated into three fractions. Varying amounts of zinc were eluted in a fourth fraction of molecular weight less than 2,000. A clear relationship was noted between the amount of copper bound to the low molecular weight fraction (m.w. ~ 10,000) and the total liver zinc concentration. The high molecular weight protein fraction (m.w. > 65,000) dominated in liver with zinc concentrations below 40 µg/g wet weight and total copper concentrations from 16 to 240 µg/g, while in liver with zinc concentrations above 40 µg/g and copper concentrations ranging from 20 to 107 µg/g, the low molecular weight metallothionein-like fraction dominated.     

Interaction of human erythrocyte multicatalytic proteinase with polycations

The multicatalytic proteinase from human erythrocytes (macropain, proteasome) is a large enzyme composed of at least six distinct subunits ranging in molecular masses from 20 to 30 kDa. As its name implies, this proteinase appears to contain multiple catalytic sites with differing specificities toward peptide substrates. Several polycationic substances, including polylysines, polyarginine, protamine and histone H1 markedly stimulated caseinolytic activity of the proteinase. Activation was instantaneous, and involved increasing the Vmax of the proteinase for casein. Prolonged preincubation with polylysine at 37 degrees C resulted in autolytic inactivation of the proteinase. The polylysine concentrations required for half-maximal activation or autolytic inactivation were the same. A 23 kDa subunit of the proteinase disappeared at the same rate as loss of catalytic activity, and with the same pH dependence and polylysine concentration dependence. These results suggest that polylysine perturbs the structure of the multicatalytic proteinase, resulting in increased catalytic activity toward substrates; and, with prolonged exposure, allowing autoproteolytic inactivation to occur. The 23 kDa subunit appeared to be required for expression of caseinolytic activity, and may therefore be a catalytic subunit of the complex having activity against casein.     

SEQ-ED: an interactive computer program for editing, analysis and storage of long DNA sequences

The rapidly growing body of sequenced DNA demands efficientcomputer programs for its analysis and storage. The programdescribed in this paper, SEQ-ED, has been designed to handlea large number of DNA sequences up to 200 kilobases [kb] longstored in a sequence library. In order to minimize the requiredstorage space, the sequences are stored in a compressed formatusing three binary digits per base. In the development of thisprogram, special care has been given to make it easy to usefor molecular biologists without any previous computer experience. Received on September 10, 1984; accepted on October 30, 1984