Immunological cross‐reactivity of fungal and yeast plasma membrane H+‐ATPase

FEBS Letters

Popolo, Laura¹  Vai, Marina¹  Alberghina, Lilia¹ 

[1] Sezione di Biochimica Comparata, Dipartimento di Fisiologia e Biochimica Generali, Università di Milano, Via Celoria 26, 20133 Milano, Italy

关键词: H+-ATPase;    2D gel electrophoresis;    Immunoblotting;    Peptide mapping;   

DOI  :  10.1016/0014-5793(86)81355-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The plasma membrane H⁺-ATPases from fungi and yeasts have similar catalytic and molecular properties. A structural comparison has been performed using immunoblot analysis with polyclonal antibodies directed toward the 102 kDa polypeptide of the plasma membrane H⁺-ATPase from Neurospora crassa. A strong cross-reactivity is observed between the fungal H⁺-ATPase and the enzyme from the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe. Structural homologies are indicated also by the analysis of the cross-reactive peptides originated by proteolytic digestion of Neurospora and S.cerevisiae purified enzymes. Neither enzyme from these two sources appears to be glycosylated by a highly sensitive concanavalin A affinity assay on blotted proteins. A glycoprotein of M _r 115000 and pI 4.8–5, which comigrates with a cell cycle-modulated protein on 2D gel, is present in partially purified preparations of plasma membrane H⁺-ATPase of S.cerevisiae and it is shown to be structurally unrelated to H⁺-ATPase.

【 授权许可】

Unknown