Intersubgeneric hybridization of soybeans with a wild perennial species,Glycine clandestina Wendl

Summary The exploitation of wild perennial species of subgenus Glycine has been formidable in soybean breeding programs because of extremely poor crossability and an early pod abortion. The combination of gibberellic acid application to hybridized gynoecia and improved seed culture media formulations resulted in a new intersubgeneric hybrid between Glycine max (L.) Merr. (2n=40) and G. clandestina Wendt. (2n=40). Of the 31 immature seeds cultured, 1 regenerated 21 plants through organogenesis while the remaining 30 failed to germinate. All the regenerated plants were similar morphologically, carried expected 2n=40, possessed hybrid isozyme patterns and were completely sterile. Complete absence of chromosome pairing was observed in 40.9% sporocytes. The occurrence of 1 to 6 loosely paired rod bivalents suggests some possibilities of allosyndetic pairing. Hybrid plants set aborted pods after backcrossing to G. max.     

Inheritance and expression of tissue-specific catalase activity during development and aging in mice

The catalase activity in the liver, kidney, lung, and blood hemolysate was measured in newborn, 21-, 70-, 175-, and greater than 400-day-old mice from the strains BALB/c, Csb, C3H/HeSnJ, C3H/S, C57BL/6J, SW, and 129/ReJ. Catalase activity was found to be highest in the liver (approximately 0.33 U/mg protein) followed by the kidney (approximately 0.13 U/mg protein), lung (approximately 0.05 U/mg protein), and blood hemolysate (approximately 0.03 U/mg protein). ANOVA analysis indicated significant differences in enzyme activity among strains and age groups studied. The developmental profiles of enzyme activity were tissue and strain specific. Catalase activity in the blood, for example, was generally higher at birth and at old age, whereas the kidney catalase activity was low at birth and increased substantially with age. Strains could be classified as normal (129/ReJ, BALB/c, C3H/HeSnJ, C3H/S), hypocatalasemic (C57BL/6J, SW), and acatalasemic (Csb) with respect to enzyme activity and it was on this basis that the inheritance of the catalase phenotype was studied using appropriate crosses. The enzyme activity level in each tissue appears to be governed by a unique set of genetic regulators/modifiers that interact with a single structural gene (Cs) or its product to produce the catalase phenotype. Some of these (e.g., Ce-1 and Ce-2) have been previously described but based on the results of various crosses reported here, more must exist that remain still uncharacterized at the molecular level. Models proposed for the inheritance of the catalase phenotype vary in complexity from single allelic differences between strains (e.g., BALB/c x Csb; blood) to a system of multiple interacting genetic determinants (e.g., BALB/c x Csb; liver) each having dominant (e.g., C57BL/6J over BALB/c; liver) and recessive components (e.g., gene(s) conferring the acatalasemic phenotype in BALB/c x Csb; blood and kidney). Such results are important and offer an interesting model to further characterize aspects of eukaryotic gene regulation.     

A SEM study of the olfactory lamellae of the catfish Heteropneustes fossilis (Bl.)

The olfactory lamellae of the catfish H. fossilis (Bl.) was studied in the scanning electron microscope. The olfactory lamellae are composed of sensory and non-sensory epithelium. The sensory epithelium contains large numbers of ciliated receptor cells, whereas the non-sensory raphe epithelium is covered with a dense mat of non-sensory cilia. It is not known whether the olfactory cilia possess receptor sites.     

Antibodies to pollen exines

A polyclonal antiserum and monoclonal antibodies have been prepared to purified pollen exines of Calocedrus decurrens Florin. The location of the antigen is in the exine, as shown by light-and electron-microscopic immunocytochemistry. The greatest reduction in antibody binding follows treatment of the exine with chemicals known to alter sporopollenin. These results provide evidence that sporopollenin is antigenic. Exines of ten species of gymnosperms and angiosperms also bound the polyclonal antiserum, indicating similarity of sporopollenin structure.     

High level of divergence of male-reproductive-tract proteins, between Drosophila melanogaster and its sibling species, D. simulans

We compared male-reproductive-tract polypeptides of Drosophila melanogaster and D. simulans by using two-dimensional gel electrophoresis. Approximately 64% of male-reproductive-tract polypeptides were identical between two randomly chosen isofemale lines from these two species, compared with 83% identity for third-instar imaginal wing-disc polypeptides. Qualitatively similar differences were found between reproductive tracts and imaginal discs when D. sechellia was compared with D. melanogaster and with D. simulans. When genic polymorphism was taken into account, approximately 10% of male- reproductive-tract polypeptides were apparently fixed for different alleles between D. melanogaster and D. simulans; this proportion is the same as that found for soluble enzymes by one-dimensional gel electrophoresis. Strikingly, approximately 20% of male-reproductive- tract polypeptides of either D. melanogaster or D. simulans had no detectable homologue in the other species. We propose that proteins of the Drosophila male reproductive tract may have diverged more extensively between species than have other types of proteins and that much of this divergence may involve large changes in levels of polypeptide expression.      

The occurrence of long chain polyprenols in leaves of plants of Rosaceae family and their isolation by time-extended liquid chromatography.

The long chain polyprenols composed of 30 and more isoprene units from leaves of plants belonging to the genera Potentilla and Rosa have been described. They occur in the form of fatty acid esters. The composition of polyprenol mixture was species dependent and its content reached ca. 0.5% wet weight. Large scale preparation of individual polyprenols from a natural polyprenol mixture was performed using time-extended liquid chromatography on the hydrophobic gel Lipidex-5000.     

Flavonoid glycosides from Cassia alata.

Two new glycosides, chrysoeriol-7-O-(2"-O-beta-D-mannopyranosyl)-beta-D-allopyranos ide and rhamnetin-3-O-(2"-O-beta-D-mannopyranosyl)-beta-D-allopyranosid e, were isolated from the seeds of Cassia alata. The structures were established on the basis of chemical evidence and spectroscopic methods, especially NMR.     

Urea metabolism in the cyanobacterium Anabaena cycadeae: regulation of urea uptake and urease by ammonia

A total of 160 Escherichia coli positive for F165 fimbrial antigen and isolated from diarrheic and septicemic animals, were examined for the presence of the pap, afa, and sfa/foc operons or related nucleotide sequences using colony hybridization. Most isolates shared DNA sequences with the pap operon sequences alone or in association with afa or sfa. Thus, our results indicate that F165-positive E. coli from diseased animals share DNA sequences with operons coding for adhesins important in human extra-intestinal disease and that multiple adhesin systems are often found in single isolates. However, 20% of the F165-positive isolates did not show any homology with the probes representing the three adhesin systems, suggesting that one of the operons responsible for F165 production could be different from the pap, sfa/foc, and afa operons.     

Cell cycle dependent variation of calmodulin in Tetrahymena

The level of calmodulin (CaM), a ubiquitous calcium-binding protein of eukaryotic cells was determined at different phases of the cell cycle in a synchronized Tetrahymena population. It was found that the concentration of CaM at G1 was approximately half of the concentration of S and this 2 x G1 level of CaM was maintained through the G2 and M stages of the cell cycle. To ascertain the role of CaM in the initiation of DNA synthesis, the cells were treated with trifluoperazine (TFP), a CaM antagonist, and EGTA (Ca2+-chelator) at the G1/S boundary. It was found that DNA synthesis was inhibited in these drug-treated cells. The uptake of the nucleotide precursor was not affected in TFP and EGTA treated cells, thus excluding the possibility of alteration in the membrane transport properties. Treatment with TFP failed to inhibit the synchronous mitotic division in Tetrahymena. The existence of a variable content of CaM through the cell cycle of Tetrahymena was demonstrated, suggesting the possible involvement of this Ca2+-binding protein in the nuclear DNA replication process.     

Molecular cloning of the cDNA for androgen-dependent sperm-coating glycoproteins secreted by the rat epididymis

cDNA clones coding for two closely related androgen-dependent sperm-coating glycoproteins secreted by the rat epididymis were selected by screening an epididymal cDNA library constructed in lambda gt 11 with affinity-purified antibody directed against the glycoproteins. The largest clone of 956 nucleotides provided coding information for a protein of 246 amino acids of which the first 19 residues comprise a putative signal peptide sequence which when cleaved would produce a mature protein of 227 residues and a molecular mass of 26 kDa. Confirmation of the identity of the clone was provided by a match between the amino acid sequence predicted from the cDNA sequence and the actual amino acid sequence determined for a tryptic peptide fragment of one of the pure glycoproteins. It is probable that the primary amino acid sequence of the two glycoproteins is identical. Northern blot and slot-blot analysis revealed that the mRNA for the glycoproteins is approximately 1250 nucleotides long and that the concentration of the mRNA in the epididymis is androgen-dependent. The glycoproteins and their mRNAs were unique to the epididymis as determined by Western and Northern blots, respectively, since signals were absent from skin, brain, liver, kidney, heart, skeletal muscle and testis. Cross-reacting proteins of slightly smaller apparent molecular mass were detected in extracts of mouse and guinea-pig epididymis, but not rabbit or bull epididymis. Comparison with existing protein data bases revealed that the epididymal glycoproteins display significant sequence homology with yeast carboxypeptidase Y.