Abstract
Antibody specific to Trichoderma reesei cellulase (65 kDa, isoelectric point, pI, 7.7) shows immuno-cross reactivity with acidic hydrolase complexes containing other cellulases, (pIapp. 3.4–4.5) when tested under conditions of 2D-electrophoresis (1st dim. PAGIF, 2nd dim. SDS-PAGE) together with Western blotting. Degradation pattern of 14C(U)-labeled G1–G5 of the 65 kDa cellulase was followed by a 2-directional oligodextrin mapping procedure. Using preparative IEF, homologous antigen portions were detected in cellulases present within acidic hydrolase complexes showing mainly identical molar weight (Mr 65 kDa and 57 kDa) but a range of charge (pI 3.4–4.5). The pattern of acidic cellulases as found after analytical 2D-electrophoresis was reconstituted by preparative IEF (pIapp. 2.7–5.1) followed by SDS-PAGE separation. Homogeneous fractions (upon IEF) gave up to 8 different polypeptides per complex upon SDS-PAGE (Mr 70−20 kDa). Charge heterogeneity of individual acidic hydrolase complexes upon IEF is discussed as one reason for ‘multiplicity’ of acidic cellulases.
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