Literature DB >> 66107

Identification of alpha1-acid glycoprotein, alpha2-macroglobulin and antithrombin III as components of normal and malignant human tissues.

S S Twining, A S Brecher.   

Abstract

alpha1-Acid glycoprotein, alpha2-macroglobulin, and antithrombin III have been identified, by immunological means, as components of the 90000 X g supernatant fraction of malignant and adjacent normal human breast, colon, and anal tissues, as well as malignant stomach and ileum. Malignant lung tissue only contained alpha1-acid glycoprotein. These protease inhibitors are immunologically equivalent to those present in human plasma.

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Year:  1977        PMID： 66107     DOI： 10.1016/0009-8981(77)90510-1

Source DB:  PubMed          Journal:  Clin Chim Acta        ISSN： 0009-8981            Impact factor:   3.786


  4 in total

1.  Large scale separation of protease inhibitors from malignant human breast tissue.

Authors:  S S Twining; A S Brecher
Journal:  Mol Cell Biochem       Date:  1977-12-29       Impact factor: 3.396

2.  Inhibition by heparin-modulated antithrombin III of amidolysis catalysed by m beta-acrosin.

Authors:  W F Long; F B Williamson
Journal:  Biochem J       Date:  1984-02-01       Impact factor: 3.857

3.  Low molecular weight proteinase inhibitors. I. Extraction and identification of activity from normal and malignant human breast tissues.

Authors:  B Waxler; F H Wezeman
Journal:  Br J Exp Pathol       Date:  1983-06

4.  Elevated alpha1-acid glycoprotein in gastric cancer patients inhibits the anticancer effects of paclitaxel, effects restored by co-administration of erythromycin.

Authors:  Yoshinao Ohbatake; Sachio Fushida; Tomoya Tsukada; Jun Kinoshita; Katsunobu Oyama; Hironori Hayashi; Tomoharu Miyashita; Hidehiro Tajima; Hiroyuki Takamura; Itasu Ninomiya; Masakazu Yashiro; Kousei Hirakawa; Tetsuo Ohta
Journal:  Clin Exp Med       Date:  2015-09-10       Impact factor: 3.984
  4 in total

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