A genetic approach to the species problem in wild potato.

Wild potatoes are native to the Americas, where they present very wide geographical and ecological distribution. Most are diploid, obligate out-crossers due to a multiallelic gametophytic self-incompatibility (S) locus that prevents self-fertilisation and crossing between individuals carrying identical S-alleles. They have two alternative modes of reproduction: sexual (by seeds) and asexual (by stolons and tubers), which provide, respectively, for genetic flexibility in changing environments and high fitness of adapted genotypes under stable conditions.

Meiotic abnormalities underlying pollen sterility in wild potato hybrids and spontaneous populations.

Wild potato species are widely distributed in the Americas, where they spontaneously grow in very diverse habitats. These species - with low chromosome differentiation - form polyploid series with 2n = 2x, 3x, 4x and 6x (x =12). They are isolated in nature by external and internal hybridisation barriers that can be incomplete, allowing hybridisation in areas of sympatry.

Experience with open-heeled Unna boot application technique.

One of the most common and effective treatments for venous stasis ulcers (VSUs) is the Unna boot dressing (UBD), first described by Unna in the 1890s. No one technique for UBD application has been documented by research to be the most effective for ulcer healing. This article discusses the open-heeled UBD application technique.

Interlobe communication in multiple calcium-binding site mutants of Drosophila calmodulin.

We have generated mutants of Drosophila calmodulin in which pairs of calcium-binding sites are mutated so as to prevent calcium binding. In all sites, the mutation involves replacement of the -Z position glutamate residue with glutamine. Mutants inactivated in both N-terminal sites (B12Q) or both C-terminal sites (B34Q), and two mutants with one N- and one C-terminal site inactivated (B13Q and B24Q) were generated.

Therapeutic walking program: an alternative to a formal vascular rehabilitation program.

A formalized 3-day-a-week structured exercise program proved unsuccessful in a regional, inner-city referral center. However, a large number of patients who needed exercise training were seen. In response to this demand, a "Therapeutic Walking Program" was designed.

Activation of four enzymes by two series of calmodulin mutants with point mutations in individual Ca2+ binding sites.

Activation of four target enzymes by two series of calmodulin Ca2+ binding site mutants has been examined. In each mutant, the conserved bidentate glutamate of one of the Ca2+ binding sites is mutated to glutamine or lysine. The enzymes studied were smooth and skeletal muscle myosin light chain kinases, adenylylcyclase, and plasma membrane Ca(2+)-ATPase.

Circular dichroism studies on calcium binding to two series of Ca2+ binding site mutants of Drosophila melanogaster calmodulin.

The Ca(2+)-induced structural changes in mutant calmodulins from Drosophila melanogaster have been studied by circular dichroism. The proteins comprise eight site-specific mutants, in which a bidentate glutamic acid (at position 12 in each Ca2+ binding loop) is replaced with either glutamine (BQ series) or lysine (BK series). Previous studies of these proteins indicate that Ca2+ binding at the mutated site is effectively eliminated by each of these substitutions, with additional effects at nonmutated sites.

Stopped-flow studies of calcium dissociation from calcium-binding-site mutants of Drosophila melanogaster calmodulin.

The kinetics of calcium dissociation from two groups of site-specific mutants of calmodulin from Drosophila melanogaster have been studied by stopped-flow kinetic methods, using the fluorescent calcium chelator 8-amino-2-[(2-amino-5-methylphenoxy)methyl]-6- methoxyquinoline-N,N,N',N'-tetraacetic acid (Quin 2). The BQ series of mutants consists of four proteins in which one of the four bidentate glutamate residues (Glu12 of each of the four calcium binding loops) has been replaced by glutamine. In the BK series of mutants, the corresponding glutamate has been replaced by lysine.

Ca2+ binding and conformational change in two series of point mutations to the individual Ca(2+)-binding sites of calmodulin.

Two series of site-directed mutations to the individual Ca(2+)-binding sites of Drosophila melanogaster calmodulin have been generated and studied. In each mutant, a conserved glutamic acid residue at position 12 in all of the Ca(2+)-binding loops has been mutated in one site. In one series the residue is changed to glutamine; in the second series the change is to lysine.

Structure of a recombinant calmodulin from Drosophila melanogaster refined at 2.2-A resolution.

The crystal structure of calmodulin (Mr 16,700, 148 residues) from Drosophila melanogaster as expressed in a bacterial system has been determined and refined at 2.2-A resolution. Starting with the structure of mammalian calmodulin, we produced an extensively refitted and refined model with a conventional crystallographic R value of 0.

Structure and sequence of the Drosophila melanogaster calmodulin gene.

A series of phage clones overlapping the single calmodulin gene locus of Drosophila melanogaster has been isolated and the exons of the gene positioned and sequenced within these clones. A calmodulin cDNA clone of the electric eel was used to identify these clones and to position the two major protein-coding exons of the gene. cDNA clones for D.