The effects of low-intensity He-Ne laser irradiation on erythrocyte metabolism.

Low-intensity laser irradiation (LILI) can improve the deformability of red blood cells (RBCs). It might be due to the LILI effects on adenosine triphosphate (ATP) level. However, ATP content may not be a valid surrogate marker for RBC deformability. The LILI effects on RBC glycolysis were studied in this paper. Hypertonic RBCs were used in this study. After 5 min irradiation with low-intensity He-Ne laser irradiation (LHNL) at 632.8 nm and 4.4 mW/cm(2), the concentration of intracellular glucose and the activities of phosphofructokinase (PFK) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) were measured, respectively. There was no significant change in intracellular glucose concentration. The activity of PFK decreased significantly, but the activity of GAPDH increased significantly. In hypertonic RBCs, LHNL irradiation may decrease the activity of energy-consuming enzymes, but increases the activity of energy-generating enzymes in glycolysis, to improve the RBC deformability.

A basic phenylalanine-rich oligo-peptide causes antibody cross-reactivity.

Glycolate oxidase (GO) and ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO) are the two enzymes that serve key functions in the photorespiration and photosynthesis of plants. A 2 kDa highly basic phenylalanine-rich oligo-peptide (BOP) binds to the surface of acidic GO via ionic and hydrophobic interactions, forming the GO-BOP complex (GC). Previously, RubisCO was thought to exist as a single species composed of a large (rbc L, 54 kDa) and a small subunit (rbc S, 14 kDa). Here we show for the first time, using 2-DE, SDS-PAGE, immunoassays and amino acid determination, that BOP also interacts with RubisCO and that many RubisCO-BOP complexes (RCs), differing in pI, hydrophobicity and activity, coexist in green leaves. GCs, RCs and crude extract from green leaves analyzed by SDS-PAGE Western blotting showed that BOP exists either in subunit-BOP complexes (GO subunit-BOP, rbc L-BOP and rbc S-BOP etc.), with a wide variation in the number and the position of BOPs bound to each subunit molecular, or alone without a binding partner. When rbc L-BOP and rbc S-BOP were assayed by SDS-PAGE, BOP was dissociated from the subunit and it self-assembled to form 37 different BOP polymers (basic phenylalanine-rich protein) whose molecular weights (M(r)s) ranged from 34.0 to 91.6 kDa, indicating that the M(r) of BOP is about 2 kDa. Thus, the addition of BOP changes the M(r) of the subunit-BOP complexes so minimally that the rbc L and rbc S run at their predicted M(r)s on SDS-PAGE. In summary, the results described here demonstrate that the presence of BOP in complexes (both subunit-BOP complex and protein-BOP complex) can cause cross-reactivity of antibodies against different proteins.