Comparative Biochemistry and Physiology Part B: Comparative Biochemistry最新文献

Cephaloscyllium ventriosum is an oviparous, bottom-dwelling shark inhabiting shallow waters from central California to Chile. Hemoglobin oxygen affinities for adult, juvenile (5 and 8 months old), and pre- and posthatch (fetal up to 10 days posthatching) individuals were determined using thin-layer spectrophotometry of hemoglobin solutions stripped of organic phosphates. Adult hemogiobin had a P₅₀ of 4.72± 0.30 mm Hg (N = 4, mean ± SE), juvenìle hemoglobin had a P₅₀ of 3.77 ± 0.65 mmHg (N = 3), and pre- and posthatch hemoglobin had a P₅₀ of 2.51 ± 0.19 mmHg (N = 6)—significantly (P < 0.05) higher than adult hemoglobin oxygen affinity. Adult blood was slightly alkaline (7.60–8.04; N = 4), had low venous P_O2 values (0.5–14.5 mmHg; N = 4), and hematocrit and hemoglobin concentration increased with age. SDS-polyacrylamide gel electrophoresis revealed slight structural differences between the hemoglobin of adult and prehatch individuals. A hemoglobin with a higher intrinsic oxygen affinity may enable fetuses of C. ventriosum to more efficiently extract oxygen from the relatively stagnant environment within the egg case.

A high-density lipoprotein (HDL) fraction was isolated from the hemolymphatic plasma of the spider Polybetes pythagoricus by density-gradient ultracentrifugation. Hydrated density (1.13 g/ml), electrophoretic mobility (SDS—PAGE) of apoproteins and lipid classes composition were determined. Lipids were identified by HP-TLC and auxiliary techniques; they were quantified by TLC-FID. The protein moiety is composed of two main apoproteins (250 and 76 kDa, respectively) and several polypeptides of low molecular weight. It resembles the apoliphorins of insects and some other arachnids. The lipid composition differs from most lipophorins. Phospholipids amount to more than 60% of total lipids, while diacylglycerols (2.4%) are supplanted by triacylglycerols (16.5%) as the main circulating energetic lipids.

A rapid, highly-specific ELISA for tyrosine kinases readily detects such activity in crude extracts prepared from rat mammary epithelial and fibroblastic cells that have been stimulated with epidermal growth factor or basic fibroblast growth factor. Tyrosine kinase activity is also found in extracts of pupae of the cotton leafworm, Spodoptera littoralis. Both the mammalian and the insect tyrosine kinases are ATP-dependent. Both cytosol and membrane-associated (Triton-X-100-soluble) fractions of Spodoptera littoralis pupae contain tyrosine kinase activity. The growth factor-stimulated tyrosine kinase activities in extracts of growth factor-stimulated rat mammary cells are inhibited by genistein and an analogue of erbstatin: methyl 2,5-dihydroxycinnamate. However, the tyrosine kinase activities present in pupae of Spodoptera littoralis are not sensitive to these inhibitors, suggesting that the major tyrosine kinases of Spodoptera littoralis pupae may be distinct from the growth factor-stimulated mammalian tyrosine kinases.

One of the urea-extractable proteins in the shell of the shrimp Pandalus borealis has been purified, and the complete amino acid sequence has been determined by the combined use of mass spectrometry and Edman degradation of the intact protein as well as of enzymatically derived peptides.

Characteristic features of the sequence are discussed and compared to sequences from insect cuticular proteins and other structural proteins.

We have identüified a carboxylesterase in A. suum that appears to be the homolog of the gut-specific C. elegansges-I menzyme. The A. suum esterase was purified and its N-terminal sequence found to be 50% identical to the C. elegansges-1 protein. We have used isoelectric focasing analysis to demonstrate that, unlike the C. elegansges-I esterase, the A. suum enzyme is not restricted to the gut but is expressed in a wide range of tissues.

The total surface lipids, including the wax particles, of the adult whiteflies of Bemisia tabaci and Trialeurodes vaporariorum were characterized. At eclosion, there were similar amounts of long-chain hydrocarbons, aldehydes, alcohols and wax esters. Within a few hours post-eclosion, long-chain aldehydes and long-chain alcohols were the dominant surface lipid components, C₃₄ on B. tabaci and C₃₂ on T. vaporariorum. Hydrocarbons, mainly n-alkanes, were minor components of the surface lipids. The major wax esters were C₄₆ on B. tabaci and C₄₂ on T. vaporariorum. The major acid and alcohol moieties in the wax esters of B. tabaci were C₂₀ and C₂₆, respectively, and of T. vaporariorum were C₂₀ and C₂₂, respectively. Both B. tabaci and T. vaporariorum had a minor wax ester composed of the fatty acid C_18:1 esterified to the major alcohols, C₃₄ and C₃₂, respectively. Bemisia were readily distinguished from Trialeurodes based on the composition of their wax particles and/or their wax esters; however, no differentiating surface lipid components were detected between biotypes A and B of B. tabaci.

The larval haemolymph of the sheep blowfly Lucilia cuprina (Weidemann) contains a juvenile hormone binding protein with a K_d for racemic JH III of 33 ± 6 nM. The density of the binding sites is 212 ± 33 pmol/mg haemolymph protein. The binding protein is equally specific for JH III and methyl farnesoate. Some natural juvenoids were ranked for their ability to displace [³H]JH III with JH III > JH II > JH I > JH III > JH III diol > JHB₃ = no detectable displacement. These data, together with displacement studies for 14 synthetic juvenoids, indicate some characteristics of the JH binding cleft. The binding protein is a high density lipophorin (density = 1.15 g/ml) and has subunit molecular weights of 228 kDa (apolipophorin I) and 70 kDa (apolipophorin II). The N-terminal amino acid sequences of the subunits have no discernible homology to any previously sequenced protein. Lipophorin-specific immunocytochemical staining occurs in a subset of fat body cells.

The phenomenon of knockdown resistance (kdr) was first noted in the housefly (Musca domestica), and has subsequently be found (i.e. kdr-type resistance) in several other insect pests including the German cockroach (Blattella germanica). This type of resistance causes insensitivity of the nervous system to pyrethroids, DDT and a limited number of sodium channel neurotoxins. In the German cockroach, kdr-type resistance is incompletely recessive, monogenic and not sex linked or due to cytoplasmic factors. Additionally, kdr-type resistance is not associated with a change in sodium channel density, kdr or kdr-type loci are tightly linked or identical to the para-homologous sodium channel locus in German cockroach, housefly and tobacco budworm (Heliothis virescens), suggesting that kdr and kdr-type resistance are due to mutations in the para-homologous sodium channel gene. kdr-Type resistance in the German cockroach appears similar, although not necessarily identical, to kdr in houseflies.