Starch-gel electrophoretic pattern

Fla. 11. Starch gel electrophoretic patterns of red cell hemolyzates with the six phenotypes representing homozygosity and heterozygosity for the three common genes at the acid phosphatase locus, P, Pb, and Pc. From Giblett (79). 

Effect of Environmental Factors on Starch Gel Electrophoretic Patterns of Human Erythrocyte Acid Phosphatase... 

Fig. 16. Starch-gel electrophoretic patterns of acetylated ovotransferrins. (A, B, and C) Iron ovotransferrin acetylated for 20, 10, and 5 minutes, respectively (D, E, and F) ovotransferrin acetylated for 20, 10, and 5 minutes, respectively (G) control ovotransferrin. Samples were the same as employed in expt A, Table I acetylation with acetic anhydride as described in text. (Biochemistry 4, 998 [1965]).

Fig. 22a-f Photograph of starch gel electrophoretic patterns of avian egg whites to which Fe59 had been added before electrophoresis, a, c, and e are photographs of the gel stained for protein with Amido black, and b, d, and f are the corresponding autoradiograms which indicate the position of the conalbumin in the starch gel. (Clark, J. R., D. T. Osuga, and R. E. Feeney (1963) Comparison of avian egg white conalbumins. (J. Biol. Chem. 238, 3621 [1963])). 

Figure 8. Starch-gel electrophoretic patterns of incubated infertile eggs. Egg whites were all white Leghorn containing globulin At. Eggs were incubated at 37°C for 6 days or stored at 2°C for 6 days (controls). Letters refer to hen (22).

Fig. 18. Starch gel electrophoretic patterns of lyophilized gastric juice from 4 normal subjects. A, 5 mg of lyophilate B, 20 mg of lyophilate. Numerals refer to individual subjects. Electrophoresis in borate buffer at pH 8.6 for 5 hours. These electrophoretic patterns were selected to illustrate the variation in cathodal staining (amido black lOB stain). From Jeffries et al. (J4).

The starch gel electrophoretic patterns obtained by Hopkinson (Hll) and his associates (H14) and subsequently by others in Harris group (H2) and elsewhere in the world (G3, K2) are shown in Fig. 1. Initial studies by Hopkinson et al. (H13) on 139 randomly selected English males and females revealed the existence of five patterns with the following frequencies in the population type A, 10.1% type BA, 46% type B, 34.5% type CA, 36% type CB, 5.8%. On the basis of genetic considerations, they predicted the existence of a sixth type, C. Lai (Ll) and his associates (L2) obtained a different distribution in a Brazilian population, but reported evidence for the existence of the type C electrophoretic pattern. Additional studies by Hopkinson (Hll) modified the incidences of the patterns slightly A, 13% BA, 43% B, 36% CA, 3% CB, 5% C, 0.016%. 

Only about 7% of the coagulating enzyme activity is retained in the cheese curd (200) the remaining activity is expelled in the whey. Recently, Dulley (200) observed that cheeses containing normal and double normal amounts of rennet showed very little difference in peptides soluble in dilute trichloroacetic acid after 10 months maturation this suggests that the amount of rennet did not significantly affect proteolytic breakdown of the cheese proteins. Furthermore, Dulley (200) did not observe a significant difference in starch gel electrophoretic patterns of cheese proteins from cheese containing normal and double normal... 

Fig. 4. Starch gel electrophoretic patterns and curve.s of radioactivity of labeled mixtures of Triton and a-LP. A a-LP-I i (2 mg), specific activity 0.5 pC/mg. B mixture of a-LP-PSt (2 mg) and Triton (40 mg) C Triton-I Si, specific activity 0.2 M-C/mg D mixture of a-LP (2 mg) and Triton-Ii i (40 mg). P = protein-stained pattern L = lipid-stained pattern (from Scanu and Oriente, 1961).

Fig. 6. Starch gel electrophoretic patterns of two pools 36 to 40, channel 2 and 41 to 45, channel 3 from the column shown in Fig. 5. Channel is the pattern of the HPL standard.

By use of starch-gel electrophoresis, the total extract of bananas, and the fractions obtained after separation on DEAE-Sephadex A-50, were found to contain six multiple forms of pectinesterase having electrophoretic patterns different from those of tomato pectinesterase.103... 

Beckman et al. (28) have studied the electrophoretic separation of the acid phosphatase activity in tissue extracts on starch gel at pH 8. They described four electrophoretic bands A, B, C, and D. Table IV (28) shows the distribution of activity in different organ extracts. The ABD pattern predominated in kidney BD in liver, intestine, heart, and skeletal muscle B in skin and D in pancreas. The C component was present in a large number of placentae but not in other adult organs. All four electrophoretic components were inhibited by d-(- -)-tartrate A contained sialic acid, D had a lower pH optimum and was more heat resistant than A, B, and C. Components C and D showed parallel electrophoretic behavior. In human skin fibroblasts grown in tissue culture, the acid phosphatase was generally high and the most common pattern was BD. Almost every culture showed some activity. The BD... 

The comparison of electrophoretic patterns of gastric juice as obtained on paper, starch gel, and agar has been studied by Cornet et al., and is illustrated in Fig. 20. 

We have already discussed the properties of human erythrocytic acid phosphatase (Section 3.3), and we pointed out that, like acid phosphate in other tissues, it may exist in several isoenzymatic forms. In 1963, Hopkinson et al. (H13) subjected hemolysates of human red cells from an English population to horizontal starch-gel electrophoresis for 17 hours at 5°C. The gels were then sliced horizontally, covered with 0.05 M phenolphthalein sodium diphosphate at pH 6.0, and allowed to incubate for 3 hours at 37°C. Five different electrophoretic patterns of acid phosphatase activity could be distinguished in different individuals. Shortly thereafter Lai and his associates (L2) confirmed these findings and discovered an additional sixth pattern which had been predicted by Hopkinson et al. (H13). The distribution of these patterns in various types of population was assiduously pursued within the next several years, and several new ones were discovered in Negro populations (G3, K2). 

Two distinct peaks of acid phosphatase activity were detected in each phenotype, but the positions of these peaks differed. For example, in phenotype A, the peaks were approximately at tubes 150 and 190 in B, at about 130, 170, and 265 in BA, at 110 and 155. In these three, the first peaks showed minor enzyme activity. In CA, there was a major peak at about tube 130 and a smaller one at about tube 170. The shape of the curves varied according to the phenotype tested. In general, these results confirmed what gel electrophoresis originally showed, namely, that there are charge differences between the various isoenzymes. The electrophoretic patterns may also be influenced by the type of buffer used to make up the starch gel (K2). 

Jeffers (T2) did electrophoretic studies on serum alkaline phosphatase in hepatobiliary and skeletal disease (Fig. 1). They found eight separate zones of alkaline phosphatase activity arranged in three distinct patterns, and suggested the use of the starch-gel zymogram in the differentiation between obstructive, metastatic, or infiltrative hepatobiliary disease, parenchymal hepatic disease, and osteoblastic disorders. 

Harris and his group (R15, R16) in London recently initiated genetic studies on human placental alkaline phosphatase, and demonstrated phenotypic differences in this enzyme. In this study, butanol extracts of alkaline phosphatase from each of 338 placentas were prepared, and the enzyme preparations were subjected to starch-gel electrophoresis at two different pH s (8.6 and 6.0). The electrophoretic patterns obtained were classified in six different groups representing six distinct phenotypes. The... 

Electrophoretic studies of the isolated erythrocuprein employing starch or polyacrylamide gels have been carried out by most of the above-cited authors. The homogeneity was not as satisfactory as in the sedimentation experiments a major component and a slightly faster component were always detectable. At the moment it is not known whether there is a genuine second component or whether the erythrocuprein decomposes during the disc-electrophoretic separation. The electrophoretic separation pattern of bovine erythrocuprein is essentially the same for erythrocuprein from human tissues (64, 68). 

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