Journal article

Publication year: 1988

Pages: 125-131

Journal: Comparative biochemistry and physiology. Part B: Comparative biochemistry

Volume number: 91

Issue number: 1

ISSN: 1096-4959

eISSN: 1879-1107

DOI Link: https://doi.org/10.1016/0305-0491(88)90123-X

Publisher: Pergamon Press

Abstract: 

1. A 50K phosphoprotein was precipitated from sponge cell extracts using an antipeptide antibody directed against the 19 carboxyterminal amino acids of the chicken proto-oncogene product pp60c-src.
2. Phosphoamino acid analysis after phosphorylation of total sponge cell protein yielded values of phosphoserine 98%, phosphothreonine 2% and phosphotyrosine 0.27%.
3. After incubation of sponge cell extracts with apparent molecular weights of 87K, 46K and 40K were detected.
4. Two-dimensional phosphoamino acid analysis revealed that the proteins were exclusively phophorylated in serine residues.
5. A comparison of partial proteolytic digestion pattern using Staphylococcus aureus V8 protease suggests that the phosphoproteins are related and/or precursors of each other.

Harvard Citation style: Hirsch-Behnam, A. and Barnekow, A. (1988) Characterization of phosphoproteins in sponge cells, Comparative biochemistry and physiology. Part B: Comparative biochemistry, 91(1), pp. 125-131. https://doi.org/10.1016/0305-0491(88)90123-X

APA Citation style: Hirsch-Behnam, A., & Barnekow, A. (1988). Characterization of phosphoproteins in sponge cells. Comparative biochemistry and physiology. Part B: Comparative biochemistry. 91(1), 125-131. https://doi.org/10.1016/0305-0491(88)90123-X