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5 recordsLinked to original sources
PubMed1977

Gene mapping in Mus musculus by interspecific cell hybridization: assignment of the genes for tripeptidase-1 to chromosome 10, dipeptidase-2 to chromosome 18, acid phosphatase-1 to chromosome 12, and adenylate kinase-1 to chromosome 2.

Chinese hamster X mouse somatic cell hybrids segregating mouse chromosomes were examined for their mouse chromosome content using trypsin-Giemsa (GTG) banding and Hoechst 33258 staining techniques. Simultaneously, they were scored for the presence of 24 mouse enzymes. The results confirm the assignments of 11 genes previously mapped by sexual genetics: Dip-1 and Id-1 to chromosome 1; Pgm-2 and Pgd to 4; Pgm-1 to 5; Gpi-1 to 7; Gr-1 to 8; Mpi-1 and Mod-1 to 9; Np-1 and Es-10 to 14. They also confirm chromosomally the assignments of 3 genes that were made by other somatic cell genetic studies: Aprt to 8; Hprt and alpha-gal to the X chromosome. But most importantly, four enzyme loci are assigned to four chromosomes that until now were not known to carry a biochemical marker which is expressed in cultured cells: Trip-1 to 10; Dip-2 to 18; Acp-1 to 12; and Ak-1 to 2. Cytogenetic examination of clones showing discordant segregation of HPRT and A-GAL, suggested the assignment of alpha-gal to region XE leads to XF of the mouse X chromosome. The cytologic studies provide a comparison between data from sexual genetics and somatic cell hybrids and validate hybrid cell techniques. They provide evidence of the reliability of scoring chromosomes by GTG and Hoechst staining and stress the importance of identifying clones with multiple chromosome rearrangements. Striking examples of norandom segregation of mouse chromosomes were observed in these hybrids with preferential retention of 15 and segregation of 11 and the Y chromosome.

Acid Phosphatase↗
PubMed1977

Human beta-glucuronidase: assignment of the structural gene to chromosome 7 using somatic cell hybrids.

beta-Glucuronidase (GUS) has become an important enzyme model for the genetic study of molecular disease, enzyme realization, and therapy, and for the biogenesis and function of the lysosome and lysosomal enzymes. The genetics of human beta-glucuronidase was investigated utilizing 188 primary man-mouse and man-chinese hamster somatic cell hybrids segregating human chromosomes. Cell hybrids were derived from 16 different fusion experiments involving cells from ten different and unrelated individuals and six different rodent cell lines. The genetic relationship of GUS to 28 enzyme markers representing 19 linkage groups was determined, and chromosome studies on selected cell hybrids were performed. The evidence indicates that the beta-glucuronidase gene is assigned to chromosome 7 in man. Comparative linkage data in man and mouse indicate that the structural gene GUS is located in a region on chromosome 7 that has remained conserved during evolution. Involvement of other chromosomes whose genes may be important in the final expression of GUS was not observed. A tetrameric structure of human beta-glucuronidase was demonstrated by the formation of three heteropolymers migrating between the human and mouse molecular forms in chromosome 7 positive cell hybrids. Linkage of GUS to other lysosomal enzyme genes was investigated. beta-Hexosaminidase (HEXB) was assigned to chromosome 5; acid phosphatase2 (ACP2) and esterase A4 (ES-A4) were assigned to chromosome 11; HEXA was not linked to GUS; and alpha-galactosidase (alpha-GAL) was localized on the X chromosome. These assignments are consistent with previous reports. Evidence was not obtained for a cluster of lysosomal enzyme structural genes. In demonstrating that GUS was not assigned to chromosome 9 utilizing an X/9 translocation segregating in cell hybrids, the gene coding for human adenylate kinase1 was confirmed to be located on chromosome 9.

Adenylate Kinase↗
PubMed1977

Purification, properties, and partial structure elucidation of a high-molecular-weight glycoprotein from cervical mucus of the bonnet monkey (Macaca radiata).

A high-molecular-weight glycoprotein has been purified from the cervical mucus of the bonnet monkey (Macaca radiata). The glycoprotein was shown to be homogeneous by electrophoresis, sedimentation equilibrium, and N-terminal group determination, and to contain 19% protein, 19% D-galactose, 18% N-acetyl-D-galactosamine, 15% N-acetyl-D-glucosamine, 11% L-fucose, 10% sialic acid, and 1% sulfate groups, corresponding to about 1800 amino acid residues and 400 carbohydrate side chains of about 9 monosaccharides. The carbohydrate chains are linked to the peptide backbone through N-acetyl-D-galactosamine and serine (or threonine) residues. Reduction with dithiothreitol and alkylation with iodoacetic acid reduced the molecular mass from 1 to 0.5 X 10(6) daltons and produced subunits having the same size, charge, and N-terminal amino acid. Electrophoretic studies suggested the presence of disulfide bonds between two chains of the glycoprotein. Degradation with alkaline borohydride gave, after fractionation on Bio-Gel P-2, fractions containing L-fucose, D-galactose, N-acetyl-D-galactosaminitol, N-acetyl-D-galactosamine, N-acetyl-D-glucosamine, and sialic acid in the ratio of 1.0:3.0:1.0:1.0:1.3:1.0. Further fractionation by electrophoresis and paper chromatography gave a charged fraction representing 13% of the original glycoprotein. Enzymic degradation and methylation studies indicated the presence of the structure alpha-Gal-(1 leads to 3)-[Fuc(1 leads to 2)]-Gal-(1 leads to 4)-GlcNAc, linked to a core component containing N-acetyl-D-galactosaminitol.

Amino Acid Sequence↗
PubMed2026

Antimicrobial susceptibility patterns of commensal fecal bacteria isolated from pigs with an intentional genomic alteration that included the selectable marker gene nptII.

INTRODUCTION: Animals with intentional genomic alterations (IGAs) hold promise for meeting increasing worldwide demand for animal-source proteins. As part of regulatory risk assessment for introducing animals with IGAs into the food chain, monitoring commensal bacterial microbiota is recommended due to concern that antimicrobial resistance genes used during IGA selection could be transferred, via horizontal gene transfer, to gastrointestinal or environmental bacterial populations, potentially contributing to antimicrobial resistance. The objective of this study was to assess the antimicrobial susceptibility patterns in commensal bacteria isolated from fecal samples of GalSafe™ pigs that have an IGA that includes the aminoglycoside resistance gene nptII. METHODS: Antimicrobial resistance rates observed in Escherichia coli, Salmonella, Campylobacter and Enterococcus isolated from GalSafe™ pigs were compared to resistance rates observed in conventional pigs at slaughter. Bacterial isolates were tested for antimicrobial resistance genes by PCR and one isolate underwent whole genome sequencing. RESULTS: In total, 137 bacterial isolates recovered from 55 fecal samples collected from 47 individual adult GalSafe™ pigs were evaluated. Prevalence of antimicrobial resistance in GalSafe™ pigs was generally similar to, or lower than, resistance prevalence reported from conventional pigs at slaughter, based on National Antimicrobial Resistance Monitoring System (NARMS) data. Higher resistance rates in GalSafe™ pigs were observed only for quinolones in Campylobacter coli (ciprofloxacin and nalidixic acid) and nitrofurantoin in Enterococcus spp. One isolate (E. coli) was positive for nptII neomycin resistance gene, the same gene used for IGA selection in GalSafe™ pigs, and the remaining 136 isolates were negative for nptII. However, the positive isolate did not appear to contain nptII derived from the GalSafe™ pig genome as the sequences flanking the gene did not match the IGA. DISCUSSION: We did not detect evidence of nptII gene transformation into bacterial species of potential human health importance in this population of GalSafe™ pigs.

NARMS↗