Substrate selectivity of squalene synthetase.

Six 1-3H-labeled analogues of farnesyl pyrophosphate have been studied as potential substrates for yeast and rat liver squalene synthetases: 2-methylfarnesyl pyrophosphate (4), 3-demethylfarnesyl pyrophosphate (5), 7,11-dimethyl-3-ethyl-2,6,10-dodecatrienyl pyrophosphate (6), 6,7,10,11-tetrahydrofarnesyl pyrophosphate (7), 4-methylthiofarnesyl pyrophosphate (8), and 4-fluorofarnesyl pyrophosphate (9). Analogues 4 and 5 are enzymatically incorporated into 11-methylsqualene (10) and 10-demethylsqualene (11), respectively, even if no farnesyl pyrophosphate is added to the incubations. None of the other analogues gives nonpolar products with either the yeast or liver enzymes. No tritium is enzymatically released to the medium from any of the analogues, indicating that they are not accepted at the first (proton exchanging) site. The data rule out formation of dead-end presqualene pyrophosphate products with analogues as first, but not as second, substrates. Implications of these results for the enzyme active-site topology and mechanism are discussed.     

Changes in protein synthesis in rats in response to endurance training

Experiments were conducted to investigate the influence of endurance exercise training on protein synthesis in skeletal muscle, heart, and liver. Training decreased incorporation of [¹⁴C]-leucine into proteins of the stromal fraction of muscle but there was no change in amino acid incorporation into proteins of the sarcoplasmic and myofibrillar fractions. Incorporation of [¹⁴C]-leucine into the protein of heart, liver, and plasma was depressed in trained rats compared to untrained rats. The specific radioactivity of [¹⁴C]-leucine was similar in tissues of trained and untrained rats and thus the depressed amino acid incorporation represents a decrease in the rate of protein synthesis. These observations demonstrate that the adaptation of muscle protein metabolism to endurance training is quite different than the alterations during work-induced hypertrophy of muscle. The difference in adaptation probably relates to the functional differences between the types of exercise. However depression of protein synthesis in trained rats is a general effect in several tissues and not an effect localized in muscle tissue.     

The Cladocera of Sri Lanka (Ceylon), with remarks on some species

The freshwater Cladocera of Sri Lanka has been revised based on the study of over 700 zooplankton samples collected from all habitat types during 1965–1980. The cladoceran fauna is represented by six families; members of the families Polyphemidae, Leptodoridae and Holopedidae are absent. The common temperate genus Daphnia is rare.Sixty-two species have been recorded from Sri Lanka. Of these, five are new records. Remarks on a few species are given with illustrations. The distribution of Cladocera in different types of habitats is discussed. The greatest species diversity was found in ponds. The Sri Lankan fauna is numerically and in species diversity typical of tropical cladoceran fauna. It resembles the southern Indian fauna very closely except for the absence in Sri Lanka of the genera Acroperus and Camptocercus.     

Spore survival during batch dry rendering of abattoir waste.

Normal batch dry rendering practice does not ensure sterile products, because bacterial spores are protected against thermal denaturation by the high fat-low water content environment which results from drying the materials at temperatures below those required for sterilization.     

On the conformational dependence of the proton chemical shifts in nucleosides and nucleotides III. Proton chemical shifts of 5′-nucleotides as a function of different conformational parameters

The variation of the chemical shift of the protons of 5′-UMP and 5′-AMP is calculated as a function of χ_CN, ψ and ? torsion angles. The shift of H8 of 5′-AMP and H6 of 5′-UMP is found to be very sensitive to the value of χ_CN. For the anti conformations the shift of these protons is more sensitive to the value of the rotation about CS′-05′ than about C4′-CS′. For the protons of the ribose the calculations show that for the C2′-endo pucker H3′ and H2′ undergo the largest chemical shift variations when ? and ψ vary. The calculated variations are considered in relation with the role of the conformation of the nucleotides in the chemical shift variation between mono and polynucleotides and between the different helical structures of polynucleotides.     

DIASTOLIC OPENING OF THE AORTIC VALVE (AV) IN A CASE OF AORTIC INSUFFICIENCY DUE TO AV FENESTRATION

A patient with severe aortic insufficiency due to fenestration of the non-coronary aortic valve leaflet is described. A preoperative echocardiogram demonstrated early closure of the mitral valve and early diastolic separation of the aortic valve leaflets. These findings disappeared after partial surgical correction and subsequent hemodynamic improvement. Premature opening of the aortic valve is common in severe aortic insufficiency.     

Aggregation of mono- and dinucleosomes into chromatin-like fibers

Three classes of chicken erythrocyte chromatin particles differing in their content of lysine-rich histones and/or spacer DNA have been studied in order to determine their ability to aggregate into complexes resembling those observed in native chromatin. The complexes have been obtained in the presence of MgCl₂ and NaCl and studied by electron microscopy. Mononucleosomes, containing spacer DNA and histones H1 and H5, give rise to thick (about 70 nm) ellipsoidal particles in the presence of 0.5 mM MgCl₂. These particles are disrupted by the addition of small amounts of NaCl (5–20 mM). On the other hand in 0.5 mM MgCl₂ dinucleosomes give rise to regular fibrous complexes of about 40 nm in diameter which are very similar to native chromatin fibers. These complexes are much more stable when NaCl is added. We conclude that for the stability of nucleosomal aggregates, similar to native chromatin fibers, a continuity of DNA structure is not required, but the presence of divalent cations, spacer DNA and lysine-rich histones is essential.