The nonspecific binding ability of polyethylenglycol (PEG) and bovine serum albumin (BSA) on modified and unmodified surfaces is quantitatively studied by a wireless-electrodeless quartz crystal microbalance (WE-QCM). PEG and BSA are important blocking materials in biosensors, but their affinities for proteins and uncoated substrates have not been known quantitatively. The WE-QCM allows quantitative analysis of the adsorption behavior of proteins on the electrodeless surfaces. Affinities of PEG, BSA, human immunoglobulin G (hIgG), and Staphylococcus protein A (SPA) for alpha-SiO(2)(quartz), Au thin film, PEG, and BSA are systematically studied by the homebuilt flow-injection system. PEG shows low affinities for the SiO(2) surface (K(A)=4.2x10(4) M(-1)) and the Au surface (K(A)=6.6x10(4) M(-1)), but BSA shows higher affinity for the SiO(2) surface (K(A)=1.4x10(6) M(-1)). Both PEG and BSA show low affinities for hIgG (K(A) approximately 1.5x10(5) M(-1)). However, the number of binding sites of PEG to hIgG is significantly larger than that of BSA, indicating that blocking for hIgG is favorably achieved by BSA, rather than PEG.

No abstract

Comparison of the entire nucleotide and deduced amino acid sequences of the attenuated hog cholera vaccine strain GPE-and the wild-type parental strain ALD Summary. We have determined the complete nucleotide sequences of a live attenuated hog cholera virus (HCV) and its progenitor strain. The viral RNA of each strain consisted of 12 298 nucleotides including untranslated regions of 373 and 228 bases at the 5' and 3' end, respectively. There was a single large open reading flame spanning 11697 nucleotides which could encode a large protein of 3 899 amino acids with a calculated molecular weight of 438-kDa. We have found 225 nucleotide difference between the two strains, of which six were located in the untranslated region. Four-sixths of these differences resulted in amino acid substitutions.

We develop the wireless-electrodeless multichannel quartz-crystal microbalance (QCM) biosensor using quartz plates of slightly different thicknesses. Their shear vibrations are simultaneously excited and detected by a pair of antenna wires to perform the noncontacting measurement. Their fundamental resonance frequencies are between 43 and 55 MHz, and vibrations at up to 10 channels are measured in liquids. Owing to high affinity of naked quartz surfaces for proteins, we immobilized various receptor proteins on different quartz plates nonspecifically and detected various antigen-antibody reactions separately. The exponential coefficient of the frequency change, rather than the amount of the frequency decrease, is found to be useful for distinguishing between specific and nonspecific binding reactions.

No abstract