Abstract: A plant cell which is resistant to a herbicidal glutamine synthetase inhibitor, wherein the resistance is caused by levels of GS activity which, when present in an otherwise herbicidal GS inhibitor sensitive plant cell, render the cell substantially resistant to the herbicidal GS-inhibitor.

Abstract: What is disclosed is a protein immunoreactive with antibodies raised against HBsAg, which protein has the formula: X-S-Y, S represents a peptide residue of the hepatitis B virus S-protein, Y is OH or NH.sub.2 and X is selected from the pre-S1/pre-S2 peptide residue, the pre S2 peptide residue and a fragment of the pre-S1/pre-S2 peptide residue containing at least a 9 amino acid portion of the C-terminal sequence of pre-S2.

Abstract: A DNA expression vector which contains the trp promotor is described. The expression vector provides for the overproduction of .beta.-lactamase. Insertion of a gene or cDNA into the .beta.-lactamase gene of the expression vector results in the over-production of a fusion protein comprising a part of the .beta.-lactamase as the N-terminal end and the protein coded for by the inserted DNA as the C-terminal end. Using the expression vector described herein, it is possible to obtain large amounts of the fusion protein. A fusion protein containing the surface antigen of Hepatitis B virus and a vaccine containing this fusion protein are also described.

Abstract: A recombinant procaryotic microorganism containing the gene coding for insulin.

Abstract: A microorganism containing a recombinant DNA transfer vector having the coding sequences for human chorionic somatomammotropin.

Abstract: Microorganism having a gene derived from a higher organism is produced by isolating cells from a higher organism containing messenger RNA, extracting the messenger RNA, synthesizing a double stranded cDNA using the messenger RNA as a template, inserting the cDNA into a plasmid and transforming a microorganism with the resultant recombinant plasmid.

Abstract: A DNA having a base sequence coding for human proinsulin and a DNA having a base sequence coding for human pre-proinsulin have been cloned, and novel recombinant DNA transfer vectors containing said cloned DNAs have been constructed. Novel microorganisms transformed by said recombinant transfer vectors have been obtained. Certain of said transformed microorganisms have demonstrated capability to express the cloned DNA's, synthesizing a protein comprising human proinsulin and a protein-comprising human pre-proinsulin.

Abstract: A method for purifying a DNA fragment of specific desired nucleotide sequence containing a restriction site, from a population of DNA molecules homogeneous in length by endonuclease cleavage and fractionation.

Abstract: Recombinant DNA transfer vectors containing codons for human somatomammotropin and for human growth hormone.

Abstract: A technique suitable for cloning a cDNA having a base sequence coding for the ACTH/LPH precursor is disclosed. The invention is exemplified by the cloning of a cDNA fragment comprising a base sequence coding for the endorphin region. The fragment, hereinafter termed the endorphin gene cDNA sequence, was obtained from cultured mouse pituitary tumor cells known to produce the ACTH/LPH precursor protein.

Abstract: A method has been discovered for purifying a specific desired DNA sequence, starting from RNA heterogeneous in length and sequence. The steps of the method include making complementary DNA transcripts of the RNA by means of an enzyme such as reverse transcriptase, subjecting the DNA transcripts to the action of one or more selected restriction endonuclease enzymes, and fractionating the fragments produced by endonuclease action according to their length. By this method it is possible to isolate homogeneous length DNA fragments complementary to RNA sequences present in the original preparation in as low a frequency as two percent. A method is also disclosed for further purifying the homogeneous length fragments and for determining their final purity. Using the disclosed methods, a DNA fragment approximately 550 nucleotides in length coding for a portion of the peptide hormone, human chorionic somatomammotropin, has been purified to greater than 99% purity.