PuSH - Publikationsserver des Helmholtz Zentrums München

Export: TXT Text RIS Endnote (RIS) BIB BibTeX
Ziegler, I. ; Maier, K.C. ; Fink, M.K.

Pteridine-binding α1-acid glycoprotein from blood of patients with neoplastic diseases.

Cancer Res. 42, 1567-1573 (1982)
Verlagsversion DOI
Closed
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
A glycoprotein was selectively enriched in the supernatant (Fraction b) obtained by alcohol and trichloroacetic acid fractionation of digitonin extracts from blood of patients with neoplastic diseases and of control subjects. Subsequent chromatography with concanavalin A:Sepharose separated a concanavalin A-reactive fraction from a concanavalin A-nonreactive one. In sodium dodecyl sulfate gel electrophoresis, the fractions from both malignant origin as well as control subjects appeared as single bands showing the same mobility. They were identical with the band obtained from commercial α1-acid glycoprotein. In Fraction b of malignant origin, greatly increased amounts of the α1-acid glycoprotein from malignant cases (AGP(M)) were found as compared to α1-acid glycoprotein from controls (AGP(C)). Furthermore, AGP(C) had a higher glycine content than did AGP(M). The electrofocusing pattern of AGP(M) showed additional bands between pH 3.7 and 4.4, whereas AGP(C) and commercial α1-acid glycoprotein focused between pH 3.2 and 3.8. In contrast to AGP(C) and to a commercial α1-acid glycoprotein, AGP(M) is characterized by a chromophoric group with maximal absorbance at 400 nm. It could be detached by treatment with 6 M guanidine hydrochloride, thus indicating a noncovalent binding. The spectral data of the separated chromophore at pH 0.5 agreed with that of a 6,7-substituted pteridine. After detachment with reducing agents, a pteridine in its 7k8-dihydro form was indicated by spectral analysis.
Impact Factor
Scopus SNIP
Altmetric
0.000
0.000
Tags
Anmerkungen
Besondere Publikation
Auf Hompepage verbergern

Zusatzinfos bearbeiten
Eigene Tags bearbeiten
Privat
Eigene Anmerkung bearbeiten
Privat
Auf Publikationslisten für
Homepage nicht anzeigen
Als besondere Publikation
markieren
Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Sprache
Veröffentlichungsjahr 1982
HGF-Berichtsjahr 1982
ISSN (print) / ISBN 0008-5472
e-ISSN 1538-7445
Zeitschrift Cancer Research
Quellenangaben Band: 42, Heft: 4, Seiten: 1567-1573 Artikelnummer: , Supplement: ,
Verlag American Association for Cancer Research (AACR)
Verlagsort Philadelphia, Pa.
Begutachtungsstatus Peer reviewed
Institut(e) Institut für Toxikologie und Biochemie
Scopus ID 0020063604
Erfassungsdatum 1982-12-31
[➜Korrektur melden]