Prolamellar bodies (PLBs) isolated from dark-grown, 6.5-d-old leaves of wheat (Triticum aesíivum L. cv. Kosack) were treated with the carboxylic acid cross-linker l-ethyl-3-[3-(diniethylaniino)propyl]carbodiimide (EDC) or with the lysině specific cross-linker 2-iniinothiolane. SDS-PAGE showed that the most prominenent cross- linked product was a dimer of the NADPH-protochlorophyllide oxidoreductase (PCR), but also larger aggregates of the polypeptide were identified by inununological detection on electro-blots. A two-dimensional diagonál gel showed that much of the cross-linking was between the PCR polypeptides. The cross-linkers induced a shift of the fluorescence peak to shorter wavelengths, a bandwidth increase of the fluorescence peak, and an increase of the fluorescence yield. In the presence of NADPH the blue shift was reduced, but the increase in the fluorescence yield still occmred. A cross-linker treatment of PLBs prior to solubilization with 1-0-n-octyl-P -D-glucopyranoside (octylglucoside) delayed, but did not prevent the spectral shifts from 657 to 646 nm and from 646 to 635 nm observed in non-cross-linked detergent- treated PLBs. The cross-linking did not prevent a spectral shift, corresponding to the Shibata shift, of Chlide. Thus the spectral shifts are not strictly coupled to disaggregation of the PCR polypeptides.