Nuclear data sheets for A = 81

Level schemes and decay characteristics are presented for all nuclei with mass number 81. Experimental data, adopted values, comparisons with theory, and arguments for spin and parity assignments are given.The adopted level schemes and decay properties are based on data received before July 1, 1974.     

Identification of carboxyl-terminal peptide fragments of parathyroid hormone in human plasma at low-picomolar levels by mass spectrometry

For decades, researchers have tried to identify the primary structures of circulating carboxyl-terminal parathyroid hormone (C-PTH) peptide fragments that may be present at only picomolar levels in human plasma. Although immunoassays and radiosequencing techniques have provided valuable fragment characterizations, no analysis has successfully determined their exact primary structures. In this work, for the first time, four human C-PTH peptide fragments, hPTH(34-84), hPTH(37-84), hPTH(38-84), and hPTH(45-84), have been identified from human plasma using MS-based methods. C-PTH peptide fragments were isolated from plasma samples by immunoaffinity extraction. The eluate was analyzed by capillary LC fractionation followed by MALDI-TOF-MS or by on-line coupling of nano-LC with ESI-TOF-MS. Both the MALDI- and the ESI-based approaches were capable of detecting C-PTH peptide fragments in human plasma at <10 pmol/L. The MALDI-TOF approach was effective in preliminary searches for C-PTH peptide fragments, but the use of high laser power limited the resolution necessary for accurate C-PTH peptide identification. The high mass resolution (10,000) and accuracy (10 ppm) attained by the ESI-TOF approach enabled unambiguous identification of these peptides. The four C-PTH peptide fragments identified in plasma samples from patients with chronic renal insufficiency were also found in the plasma of healthy women receiving recombinant human PTH either by subcutaneous injection or by intravenous infusion. This newly developed analytical capability should greatly enhance the understanding of PTH metabolism and parathyroid gland function.     

Dynamic rheology and thermal transitions of surimi seafood enhanced with ω-3-rich oils

Surimi-based seafood products are widely accepted and enjoyed worldwide. The U.S. consumption increased in 1980s; however, it leveled thereafter. Food products nutrified with ω-3 polyunsaturated fatty acids (PUFAs) are in increasing demand due to demonstrated health benefits. Currently, surimi seafood is not nutrified with ω-3 PUFAs. In the present study, surimi seafood was nutritionally-enhanced with ω-3 PUFAs-rich oils (flaxseed, algae, menhaden, krill, and blend). Protein endothermal transitions, heat-induced gelation (elastic modulus, G′), and fundamental texture properties (shear stress) of Alaska pollock surimi nutrified with ω-3 PUFAs-rich oils (flaxseed, algae, menhaden, krill, and blend) were determined and compared to Alaska pollock surimi without oil (control). Differential scanning calorimetry showed that oil addition enhanced thermal transition of actin and did not compromise the transition of myosin. The addition of oil improved heat-induced protein gelation as demonstrated with dynamic rheology. Elastic modulus increased when oil was added. There were no differences (P > 0.05) in shear stress between surimi gels with and without oil, indicating that nutrification with ω-3 PUFAs-rich oils within the ranges tested did not alter gel strength. This study demonstrates that the nutritional value and gelation of surimi seafood can be enhanced without altering texture properties by addition of ω-3 PUFAs-rich oils.     

Effects of apoE gene polymorphism on Lp(a) concentrations depend on the size of apo(a): a study of 466 white men

Polymorphisms in the genes for the low-density lipoprotein (LDL) receptor ligands, apolipoprotein E (apoE), and apolipoprotein B (apoB) are associated with variation in plasma levels of LDL cholesterol. Lp(a) lipoprotein(a) [Lp(a)] is LDL in which apoB is attached to a glycoprotein called apolipoprotein(a) [apo(a)]. Apo(a) has several genetically determined isoforms differing in molecular weight, which are inversely correlated with Lp(a) concentrations in blood. The interaction of apo(a) with triglyceride-rich lipoproteins differs with the size of apo(a), and therefore the effects of apoE gene polymorphism on Lp(a) levels could also depend on apo(a) size. We have investigated the possible effect of genetic variation in the apoE and apoB genes on plasma Lp(a) concentrations in 466 white men with different apo(a) phenotypes. Overall there was no significant association between the common apoE polymorphism and Lp(a), but in the subgroup with apo(a)-S4, concentrations of Lp(a) differed significantly among the apoE genotypes (P = 0.05). Lp(a) was highest in the apoE genotypes epsilon 2 epsilon 3 and epsilon 3 epsilon 3 and lowest in genotype epsilon 3 epsilon 4, and the apoE polymorphism was estimated to account for about 2.4% of the variation in Lp(a). In contrast, in the subgroup with apo(a)-S2 Lp(a) was significantly lower (P = 0.04) in apoE genotype epsilon 2 epsilon 3 than in genotype epsilon 3 epsilon 3. Lp(a) concentrations did not differ among the XbaI (P = 0.65) or SP 24/27 (P = 0.26) polymorphisms of the apoB gene. The expected effects of both apoE and apoB polymorphism on LDL levels were significant in the whole population sample and in subjects with large-sized apo(a) isoforms (P < 0.01), whereas no effect was seen in those with low molecular weight apo(a) isoforms. We conclude that the influence of apoE genotypes on Lp(a) concentrations depends on the size of the apo(a) molecule in Lp(a), possibly because both apo(a)-S4 and apoE4 have high affinity for triglyceride-rich lipoproteins and may be taken up and degraded rapidly by remnant receptors.