Identification of human pituitary growth hormone variants by mass spectrometry.

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Identification of human pituitary growth hormone variants by mass spectrometry. / Kohler, Maxie; Thomas, Andreas; Püschel, Klaus; Schänzer, Wilhelm; Thevis, Mario.

in: J PROTEOME RES, Jahrgang 8, Nr. 2, 2, 2009, S. 1071-1076.

Publikationen: SCORING: Beitrag in Fachzeitschrift/ZeitungSCORING: ZeitschriftenaufsatzForschungBegutachtung

Harvard

Kohler, M, Thomas, A, Püschel, K, Schänzer, W & Thevis, M 2009, 'Identification of human pituitary growth hormone variants by mass spectrometry.', J PROTEOME RES, Jg. 8, Nr. 2, 2, S. 1071-1076. <http://www.ncbi.nlm.nih.gov/pubmed/19123788?dopt=Citation>

APA

Vancouver

Kohler M, Thomas A, Püschel K, Schänzer W, Thevis M. Identification of human pituitary growth hormone variants by mass spectrometry. J PROTEOME RES. 2009;8(2):1071-1076. 2.

Bibtex

@article{e2013432a5e24cf28860165cb50b2fcf,
title = "Identification of human pituitary growth hormone variants by mass spectrometry.",
abstract = "The heterogeneity of human endogenous growth hormone (GH) is used in doping control analysis to distinguish it from the homogeneous recombinant analogue in plasma samples. Pituitary GH variants were characterized by gel electrophoresis and mass spectrometry. Besides 22 and 20 kDa isoforms, fragments of 9 and 12 kDa were identified and a glycosylated 23 kDa GH variant was elucidated to bear a HexHexNac 2 NeuAc modification presumably located at Thr 60.",
author = "Maxie Kohler and Andreas Thomas and Klaus P{\"u}schel and Wilhelm Sch{\"a}nzer and Mario Thevis",
year = "2009",
language = "Deutsch",
volume = "8",
pages = "1071--1076",
journal = "J PROTEOME RES",
issn = "1535-3893",
publisher = "American Chemical Society",
number = "2",

}

RIS

TY - JOUR

T1 - Identification of human pituitary growth hormone variants by mass spectrometry.

AU - Kohler, Maxie

AU - Thomas, Andreas

AU - Püschel, Klaus

AU - Schänzer, Wilhelm

AU - Thevis, Mario

PY - 2009

Y1 - 2009

N2 - The heterogeneity of human endogenous growth hormone (GH) is used in doping control analysis to distinguish it from the homogeneous recombinant analogue in plasma samples. Pituitary GH variants were characterized by gel electrophoresis and mass spectrometry. Besides 22 and 20 kDa isoforms, fragments of 9 and 12 kDa were identified and a glycosylated 23 kDa GH variant was elucidated to bear a HexHexNac 2 NeuAc modification presumably located at Thr 60.

AB - The heterogeneity of human endogenous growth hormone (GH) is used in doping control analysis to distinguish it from the homogeneous recombinant analogue in plasma samples. Pituitary GH variants were characterized by gel electrophoresis and mass spectrometry. Besides 22 and 20 kDa isoforms, fragments of 9 and 12 kDa were identified and a glycosylated 23 kDa GH variant was elucidated to bear a HexHexNac 2 NeuAc modification presumably located at Thr 60.

M3 - SCORING: Zeitschriftenaufsatz

VL - 8

SP - 1071

EP - 1076

JO - J PROTEOME RES

JF - J PROTEOME RES

SN - 1535-3893

IS - 2

M1 - 2

ER -