4863866 Bradyrhizobium japonicum mutants exhibiting superior soybean nodulation

4863866 Bradyrhizobium japonicum mutants exhibiting superior soybean nodulation

PATENT ABSTRACTS 369 clones on the culture medium according obtained locational information. BRADYRHIZOBIUM JAPONICUM MUTANTS EXHIBITING SUPERIOR S...

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PATENT ABSTRACTS

369

clones on the culture medium according obtained locational information.

BRADYRHIZOBIUM JAPONICUM MUTANTS EXHIBITING SUPERIOR SOYBEAN NODULATION

to the

4865968 DNA SEQUENCING

Robert M Zablotowicz, Robert G Upchurch, James Ligon, Toronto, NC, Canada assigned to Lipha Chemicals Inc Mutant strains of Bradyrhizobium japonicum having enhanced nodulation properties were created by transposon mutagenesis of known Bradyrhizobium japonicum strain I-l 10. The mutant strains grow well in a yeast-extract mannitol medium, produce extracellular polysaccharides at a level greater than the parent strain under appropriate conditions, are capable of growth on a nutirent medium containing a normally inhibitory amount of succinic acid, and contain a 21 Kdalton protein absent from the parent strain. Such strains can be used to inoculate soil in which soybean plants are grown, resulting in improved plant yields.

4865967 AUTORADIOGRAPHIC GENE SCREENING METHOD Hisashi Shiraishi, Junji Miyahara, Hisatoyo Kato, Minami Ashigara, Japan assigned to Fuji Photo Film Co Ltd An autoradiographic gene-screening method employing a hybridization process, which comprises: (I) a step of transferring a portion of genetic clones cultured on a culture medium onto a filter to fix them thereonto; (2) a step of hybridizing the genes of said clones fixed onto said filter with radioactively labeled probes; (3) a step of obtaining two dimensional information on the location of the radioactively labeled substances on the filter which comprises placing said filter having been subjected to the hybridization and a stimulable phosphor sheet in layers for a given period of time to cause said stimulable phosphor sheet to absorb at least a portion of radiation energy emitted by the radioactively labeled substances on the filter, exciting said sheet with an electromagnetic wave to release the radiation energy stored in said sheet as stimulated emission, and detecting the stimulated emission to obtain a locational information on the radioactively labeled substances on the filter; and (4) a step recovering the

Leslie E Orgel, James W Patrick assigned to The Salk Institute for Biological Studies A first mixture is prepared that contains labeled chain fragments which each has a common end adjacent to a primary nucleotide and a termination at a position from the primary through an nth nucleotide, the first mixture containing nucleotide chain fragmentrof each length from termination at the primary through termination of the nth nucleotide. A second mixture is prepared that contains labeled chain fragments beginning at the common end and terminating at positions from the first through the nth nucleotide, the second mixture containing chain fragments of each length terminating wherever either a first or a second of the four nucleotides occurs. A third mixture is prepared that contains labeled chain fragments beginning at the common end and terminating at a position from the first through the nth nucleotide, the third mixture containing chain fragments of each length terminating wherever the first or a third of the four nucleotide sequences occurs. The chains are electrophoresed with the first mixture as the center lane. This three-lane system provides a unique band pattern for each of the four nucleotides and permits the sequence to lx read merely by directly comparing each of the flanking lanes with the fully stepped center lane. This system has important advantages in reducing reading errors, particularly when read with computerassisted scanning apparatus.

4865974 BACTERIAL METHIONINE N-TERMINAL PEPTIDASE Arie Ben-Bassat, Keith A Bauer, Shing Chang, Sheng-Yun Chang assigned to Getus Corporation Methods for obtaining N-terminal methioninefree proteins involve a novel E. coli methionine amino pcptidase. The method is capable of in vitro or in vivo application. For in vivo application, a plasmid-borne DNA encoding the peptide is expressed in a bacterial host.