Semen controlled-release capsules allow a single artificial insemination in sows

Controlled-release capsules containing boar spermatozoa were developed to extend the preservation time of spermatozoa and maximize the efficiency of a single artificial insemination. A large trial (4245 sows) was performed with these capsules using double/triple conventional artificial insemination as a control. The effect of treatment on pregnancy diagnosis, delivery, and born piglets was investigated, with allowance being made for considering season, spermatozoa amount, and the weaning-to-estrus interval as confounding variables. The same pregnancy rate and prolificacy were obtained by two insemination techniques, and a higher parturition frequency was reached with capsules. The reproductive performance in pigs has therefore been optimized by a single instrumental insemination with controlled-release capsules.     

Getting to the end of RNA: Structural analysis of protein recognition of 5′ and 3′ termini

The specific recognition by proteins of the 5′ and 3′ ends of RNA molecules is an important facet of many cellular processes, including RNA maturation, regulation of translation initiation and control of gene expression by degradation and RNA interference. The aim of this review is to survey recent structural analyses of protein binding domains that specifically bind to the extreme 5′ or 3′ termini of RNA. For reasons of space and because their interactions are also governed by catalytic considerations, we have excluded enzymes that modify the 5′ and 3′ extremities of RNA. It is clear that there is enormous structural diversity among the proteins that have evolved to bind to the ends of RNA molecules. Moreover, they commonly exhibit conformational flexibility that appears to be important for binding and regulation of the interaction. This flexibility has sometimes complicated the interpretation of structural results and presents significant challenges for future investigations.     

Investigation on the asymmetrical induced yields in90Sr-90Y-beta-irradiated D- and L-alanines

This investigation was aimed to prove the asymmetrical interactions of polarized electrons from⁹⁰Sr-⁹⁰Y-beta-decay with D- and L-alanines. By use of ESR measurements, it was determined that the asymmetrical yields induced in⁹⁰Sr-⁹⁰Y-beta-irradiated alanines are 10% more in D-alanine than in L-alanine.     

Larval salt gland ofArtemia salina nauplii

Summary Naupliar brine shrimp (Artemia salina) have been used to study the salt-dependent regulation of protein synthesis. Measurement of thein vivo rates of protein synthesis was found to be very complex and dependent upon the leucine concentration of the external medium, rate of leucine entry and time of equilibration between various internal pools of leucine. Techniques were developed which permitted the measurement of rates of incorporation of^l4C-L-leucine into naupliar protein at various salinities under conditions that provided the organisms with a constant internal specific activity. It was found that salinities over 0.25 M NaC1 caused decreased rates of protein biosynthesis. A comparison of the rate of protein synthesis in the presence of chloramphenicol, cycloheximide and puromycin indicated that qualitative as well as quantitative changes in synthesis of proteins was directed by the external salinity. A feed-back mechanism based on the partitioning of available energy (ATP) between ion transport and protein synthesis is hypothesized.This work was supported by AEC grant RLO 2227-T13-1. The authors wish to express their gratitude to Prof. Robert R. Beoker and Robert L. Howard, Department of Biochemistry and Biophysics, for the technical assistance and use of the automatic amino acid analyzer in collecting data presented in Table 1 and Table 2.     

Physico-chemical properties influence the functions and efficacy of commercial bovine lactoferrins

Human and bovine lactoferrin (hLf and bLf) are multifunctional iron-binding glycoprotein constitutively synthesized and secreted by glandular epithelial cells and by neutrophils following induction. HLf and bLf possess very high similarity of sequence. Therefore, most of the in vitro and in vivo studies are carried out with commercial bLf (cbLf), available in large quantities and recognized by Food and Drug Administration (FDA, USA) as a safe substance. Physico-chemical heterogeneity of different cbLf preparations influences their effectiveness. CbLf iron-saturation affects thermal stability and resistance to proteolysis. Moreover, other metal ions such as Al(III), Cu(II), Mg(II), Mn(II), Zn(II) are chelated by cbLf, even if at lower affinity than Fe(III). Ca(II) is also sequestered by the carboxylate groups of sialic acid present on glycan chains of cbLf thus provoking the release of LPS, contributing to bactericidal activity. Similarly to more than 50% of eukaryotic proteins, cbLf possesses five N-glycosylation sites, also contributing to the resistance to proteolysis and, putatively, to the protection of intestinal mucosa from pathogens. CbLfs possess several functions as anti-microbial, anti-biofilm, anti-adhesive, anti-invasive and anti-inflammatory activities. They are also relevant modulators of iron and inflammatory homeostasis. However, the efficacy of cbLfs in exerting several functions can be erratic mainly depending from integrity, degree of iron and other metal ions saturation, N-glycosylation sites and chains, desialylated forms, Ca(II) sequestration, presence of contaminants and finally the ability to enter inside nucleus.