We analyzed cholinesterase (ChE) isoenzyme patterns of various laboratory animal species using electrophoresis to explore possible species-related variations and also to determine if there is a relationship between the ChE activity and the ChE isoenzyme pattern.
The laboratory animals that we used were Standard Wistar and Spraque-Dawley rats, Djungarian hamsters, Hartley guinea pigs, Japanese white rabbits (JW-NIBS strain), Beagle dogs, Japanese monkeys, Yorkshire pigs, Thoroughbred horses and Japanese quail. The ChE isoenzyme patterns were determined using polyacrylamide gradient gel electrophoresis (PAG-EP). The activity of serum ChE was measured using Ellman's method. The ChE isoenzymes of Wistar and Sprague-Dawley rats consisted of six separate fractions and sex- and/or age-related differences in the number of fractions were not observed. However, a sex-related variation was observed in the proportions of individual ChE isoenzyme bands for both rat strains. Also a sex-related difference was demonstrated in the serum ChE activity. The number of fractions of the ChE isoenzyme exhibited a species-related variations in the other animals. Hamsters, guinea pigs, rabbits, dogs, monkeys, pigs, horses and quails had 4, 3, 4, 3-5, 3, 3, 4 and 3 ChE isoenzyme bands, respectively. However, with the exception of the rats, the hamsters, guinea pigs, rabbits, dogs, monkeys, pigs, horses and quail did not show any sex-related difference in the proportions of their ChE isoenzyme bands or in the ChE activities.
Therefore, it appears that there is a relationship between the serum ChE activity and the proportion of ChE isoenzyme bands. These results suggest a possible species-related variation in the mode of polymerization of serum ChE subunits that constitute the ChE isoenzymes.

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A Mathematical theory of steady state of moving boundary electrophoresis was described in detail and the theory was applied to the Tiselius' moving boundary of serum albumin in Barbital and phosphate buffers. The theory showed that the steady boundary could be formed in the ascending but not in the descending boundary. The changes of concentrations of the protein and buffer components, conductance and pH along the direction of electrophoresis were calculated for the ascending boundary and the results were in agreement with experiments.

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The soluble proteins extracted from albumen glands and eggs of land snails, Euhadra peliomphala, E. subnimbosa and E. quaesita in feeding, were analyzed using SDS polyacrylamide gel electrophoresis (SDS-PAGE) and O'Farrell's two dimensional gel electrophoresis (2D-PAGE).
Although SDS-PAGE did not show any clear differences of the protein composition in three species, species specifc polypeptides were detectable by the use of 2D-PAGE. Moreover, 2D-PAGE patterns showed that albumen glands and eggs shared most of the major polypeptide spots.
On the basis of the polypeptide mapping methods, all the polypeptides in albumen glands and in eggs were classified into 14 groups. The common polypeptide groups (13 groups of them) in both albumen glands and eggs, that might migrate from albumen glands to eggs during oogenesis, were demonstrated on the polypeptide maps.

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Lectin in egg-mass of fresh water snail, Biomphalaria glabrata (PR strain), was purified and studied biochemically.
This lectin (B. glabrata agglutinin, BGA) had agglutination activity against human A type and B type erythrocyte, whereas it did not agglutinate human O type erythrocyte and rabbit erythrocyte. Since this agglutination activity was inhibited most strongly with N-Acetyl-D-glucosamine (GlcNAc) of all the tested saccharides, purification of the BGA was carried out using affinity chromatography with GlcNAc-Sepharose and gel chromatography with Sepharose 4B.
Electrophoresis of 4-15% polyacrylamide gel showed that purified BGA was constituted with two protein components. Either of them had pI 5.1, and their M. W. was roughly estimated to be more than 150, 000.
Moreover, to study polypeptide components of BGA, purified BGA was analyzed using SDS polyacrylamide gel electrophoresis (SDS-PAGE) and O'Farrell's two dimensional gel electrophoresis (2D-PAGE). SDS-PAGE pattern of purified BGA showed one polypeptide band, but two polypeptide spots, one was major and the other was minor, were found in 2D-PAGE pattern. The major polypeptide component of BGA had pI 5.1 and M. W. 18, 200, while minor component had pI 4.9 and the same M. W. as the major one.

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We examined a logic to detect lactate dehydrogenase (LDH) subunit deficiency heterozygote. From laboratory screening, simulation of subunit deficiency, and family analyses, subunit deficiency did not always show low serum LDH activity, however, showed a characteristically unusual serum LDH isozyme pattern.
By western blotting using anti-H subunit antibody, we tried to detect LDH isozyme I and II in red blood cells. The results were that there was no heterotetramer with normal H subunit in M subunit deficiency homozygote. Additionally, making a comparison between activity and protein concentration, there was no variant M subunit in M subunit deficiency heterozygote, while, there is variant H subunit in H subunit deficiency heterozygote.

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Serum ultrafiltrate was obtained from hemodialysis patient by using an extra corporeal ultrafiltration method equipped with a hollow fiber dialyser, and electrophoresed on the SDS-polyacrylamide gel having a high resolving power in the low molecular weight region less than 40 KD. From immunological property and determination of the sequence of N-terminal 16 amino acids, 25 KD protein was identified to be apo A-I lipoprotein. In contrast to 26 KD apo A-I in HDL, 25 KD apo A-I existed in free state largely as dimer, as revealed by gel filtration. In two-dimensional electrophoresis, 25 KD protein focused as two bands, pI 5.56 and 5.71, being in accord with electrofocusing behavior of apo A-I from HDL⁵⁾.

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In the present case, LDH enzyme was bound to IgG to form a complex. The LDH-IgG (lambda) complex became macromolecular and showed a marked decrease in the enzymatic activity. This inhibitory effect on LDH was apparently caused by the so-called abnormal IgG that inactivated the H(B)-and M(A)-subunits of LDH. It was suggested that the IgG modified by sialic acid was involved in the LDH inactivation.

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