American anthropologists looking through Taiwanese culture

Conclusion Anthropologists have too often supported — in their words, in their presences, and in their deeds — the paternalistic claims of rulers suppressing the very cultures they want to study. Much anthropological work legitimates substitution of the language of Beijing for Hakka and Holo, justifies ignoring Taiwanese culture, and subordinates consideration of its specific features to writing about Chinese civilization, just as Taiwanese are economically and politically subordinated to the ethnic minority dictatorship which still rules Taiwan under the fiction of being the government of China. The China that Arthur Wolf and others serve in return for support of their research from what purports to be the Republic of China is an egregious, but unfortunately not unique, example.Stephen O. Murray is with El Instituto Obregón, San Francisco, California. Keelung Hong is with the Cancer Research Institute, University of California, San Francisco.As is normal in anthropology, except for Taiwan, native terms are romanized in the native language (in the first author's recording of the second author's Daidiong idiolect, without indication of the extremely intricate tone differentia), not in the official language of the ethnic oligarchy ruling Taiwan (Beijinghua). Mainland place names are rendered in pinyin. We have followed the convention of treating Chinese and Taiwanese personal names as two words, because books are catalogued with such names. If personal names are considered as two words (an imposition of the hoary dogma that words in Sino-Tibetan languages are monosyllabic), it seems to us that both words should be capitalized. For Taiwanese placenames, we have not separated syllables by dashes or by spaces.     

Genomic characterization ofCampylobacter jejuni by field inversion gel electrophoresis

The genome ofCampylobacter jejuni was characterized by field inversion gel electrophoresis (FIGE) after digestion with three rare-cutting restriction endonucleases. The restriction enzymesSac II (5-CCGCGG),Sal I (5-GTCGAC), andSma I (5-CCCGGG) were found to produce 13, 5, and 8 fragments respectively from theC. jejuni genome. The fragment sizes ranged from 1.6 kb to 1300 kb, which gaveC. jejuni a genome size of approximately 1900 kb. Furthermore, thegly A and rRNA genes ofC. jejuni were localized to specific fragments by use of Southern analysis, and thegly A gene was shown to be closely linked to one of the three rRNA genes.     

Plant-microbial interaction under gnotobiotic conditions: A scanning electron microscope study

Inoculation of canola seeds withPseudomonas putida GR12-2 stimulates root elongation under gnotobiotic conditions. Transformation ofP. putida GR12-2 with the broad-host-range plasmid pGSS15 abolishes the enhancement of root elongation. With scanning electron microscopy it was found that both transformed and nontransformedP. putida GR12-2 are capable of binding to canola seed coats. In addition, it was observed that 4 days after the initial inoculation the roots of bothP. putida GR12-2- and GR12-2/pGSS15-treated seedlings were free of adhering bacteria despite the fact that it was subsequently shown that both bacterial strains are capable of binding to roots. Thus, adhesion to roots is not necessary for the initial phase of enhanced root elongation that is induced byP. putida GR12-2 under gnotobiotic conditions.     

Simultaneous purification and characterization of aspartate aminotransferase isoenzymes from chicken liver

Cytosolic and mitochondrial isoenzymes of aspartate aminotransferase (EC 2.6.1.1) were purified to homogeneity from chicken liver, without previous fractionation of the subcellular components. The procedure includes initial heat treatment and ammonium sulfate fractionation. The two isoenzymes can then be separated by a DEAE-Sepharose chromatography using a linear gradient of L-aspartate (reaction substrate). The separated fractions can be further purified by a parallel step with HA-Ultrogel prior to octyl-Sepharose (c-AAT) and CM-Sepharose (m-AAT) chromatographies. Michaelis constants, pI values, inhibition by adipate and subforms generation with time were studied for both isoenzymes.     

Identification of the products and nucleotide sequences of two regulatory genes involved in the exogenous induction of phosphoglycerate transport in Salmonella typhimurium.

We describe the determination of the nucleotide sequence of two genes (pgtB and pgtC) contained within the 3.4-kilobase DNA segment sandwiched between the transporter gene, pgtP, and the regulatory gene, pgtA. These two genes are involved in the regulation of expression of phosphoglycerate transport in Salmonella typhimurium. The sequence indicates the presence of two large open reading frames, potentially coding for two polypeptides of 397 and 593 amino acid residues. The two gene products were identified by using the bacteriophage T7 RNA polymerase-T7 promoter coupled system of Tabor and Richardson, and the observed apparent mass of 45 and 69 kilodaltons correlated well with the respective open reading frames. The cellular location of these two polypeptides was directly determined, and the polypeptides were found to be associated with the membrane. Although overall these polypeptides appear to be hydrophilic, there is one hydrophobic transmembrane segment in the smaller polypeptide and four such segments in the larger polypeptide which can account for their association with the membrane. In the accompanying paper, we present genetic evidence that pgtB and pgtC genes are involved in the induction of the pgtP expression by modulating derepressor activity.     

Macrophage colony-stimulating factor is produced by human T lymphoblastoid cell line, CEM-ON: identification by amino-terminal amino acid sequence analysis

A subclone, designated CEM-ON, derived from an azaguanine-resistant human leukemic T cell line, CEM-AG(R), constitutively secretes a colony-stimulating factor (CSF) which stimulates the production of macrophages from murine bone marrow progenitor cells. This CSF has been purified from serum-free conditioned medium. Highly purified CEM-ON CSF with a specific activity of 4.7 X 10(7) units/mg protein was obtained. Amino-terminal sequence analysis showed that the first 27 amino acids were identical to the amino-terminal sequence of the M-CSF (CSF-1) based on the cDNAs for human M-CSF. On SDS-PAGE analysis, CEM-ON CSF had an apparent molecular weight of 33,000-43,000; following reduction with 2-mercaptoethanol, this migrated as a 20,000-24,000 subunit, suggesting a homodimer structure. These results show that a human T cell line, CEM-ON, secretes M-CSF into its medium.