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Isolation and characterization of angiogenin, an angiogenic protein from human carcinoma cells.
The first human tumor derived protein with in vivo angiogenic activity to be obtained in pure form has been isolated from serum-free supernatants of an established human adenocarcinoma cell line
Amino acid analysis utilizing phenylisothiocyanate derivatives.
Using phenylisothiocyanate as the reagent, detection limits under 1 pmol can be routinely achieved, allowing the analysis of submicrogram protein samples, giving the analyst the first realistic alternative to ion-exchange analysis without compromising desirable features of the traditional methodology.
Amino acid sequence of human tumor derived angiogenin.
The amino acid sequence and disulfide bond pairing of human tumor derived angiogenin, the first tumor angiogenesis factor to be isolated in pure form from human sources, have been determined by
Chromatographic separation of 1-phenyl-3-methyl-5-pyrazolone-derivatized neutral, acidic and basic aldoses
Abstract Analysis, by HPLC, of reducing monosaccharides as their 1-phenyl-3-methyl-5-pyrazolone derivatives is attractive owing to its sensitivity of detection and the generation of single
Isolation and characterization of a human colon carcinoma-secreted enzyme with pancreatic ribonuclease-like activity.
The physical, functional, and chromatographic properties of the serum ribonuclease are essentially identical with those of the tumor enzyme; however, the liver enzymes, however, differ markedly from the HT-29 rib onuclease.
Sequence of the cDNA and gene for angiogenin, a human angiogenesis factor.
The amino acid sequence of human angiogenin is about 35% homologous with human pancreatic ribonuclease, and the amino acid residues that are essential for the activity of ribonUClease are also conserved in angiogenesis factor.
Actin is a binding protein for angiogenin.
The results indicate that the angiogenin binding protein is a cell surface actin and suggest that the reaction between angiogensin and this actin is an essential step in theAngiogenesis process induced by angiogenicin.
Comparison of amino acid analyses by phenylisothiocyanate and 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate precolumn derivatization.
An extensive retrospective comparison was conducted of the long-term repeatability and consistency of amino acid analyses using phenylisothiocyanate and 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate precolumn derivatization, and the superiority of AQC over PTC methodology was clearly apparent.
The angiogenins
  • D. J. Strydom
  • Medicine
    Cellular and Molecular Life Sciences CMLS
  • 1998
Examination of the many expressed sequence tags published in the public databanks revealed that angiogenin and RNase-4 (the most evolutionarily conserved RNase), share various identical 5′-untranslated regions on their sets of messenger RNAs, suggesting that their genes are in very close proximity on chromosome 14 and that they are products of differential splicing.
Isolation of angiogenin from normal human plasma.
It is reported that a protein which is physically and functionally identical with angiogenin is present in normal human plasma and can be purified to homogeneity by CM 52 and Mono S cation-exchange chromatography.