鶏 Oxyhemoglobin 中から単離した Aspartate-および Alanine-aminotransferase 系アミノ基転移酵素の活性とその物理化学的性状について

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The results of previous studies26?29) led to the conclusion that components 2-c and4-d revealed from adult chicken oxyhemoglobin by disc electrophoretic analysis??"")must play a significant role as carriers of F-GOT, R-GOT, F-GPT, R-GPT, and GRT-a 5 @.2 0 = 2?3 , 2 5, 2 T X 3 1 ).In recent years, more detailed information on this aspect was obtained by the authorsmethod introduced in this paper.The results of the present investigation are summarized as follows.I. By use of disc electrophoresis, component 2-c at relative positions 67 and 68, andcomponent 4-d at various relative positions 28, 29 and 30 were subfractionated from adultchicken oxyhemoglobin under six general terms, as evidenced in Table I.2. The isoelectric point of component 2-c ranged from 4.4 to 5.8 of pH and thatof component 4-d from 5.2 to 6.9. The values of both components were within the acidpH range.3. The average values of sedimentation constant estimated on components 2-c and4-d were 3.5 and 10.9, respectively.4. In an absorbancy of the Soret absorption band, it was clear that component 2-cwas closely related to Fe-protoporphyrin and involved particular kinds of R-GOT andR-GPT, in addition to CRT-ase. Component 4-d showed a Soret absorption peak relatedto pyridine protoheme and involved F-GOT, CRT-ase, and reversible GPT.5. The actual amounts of N, S, and Fe in component 4-d were smaller than thoseof component 2-c. Using a factor of l as the basis of total amount of Fe involved ineach component for converting N and S contents to Fe content, the molar ratio of Nand S to Fe was described in this writing.Besides, determination was performed on hexosamine, phospholipid, and cholesterol" content. It was demonstrated that (1) component 2-c. was mucoid, (2) component 2-c.and its subfrartion (SF) were mucoprotein, (3) component 4-d was a substance close toglucoprotein, (4) the actual amount of phospholipid in component 2-c. was larger thanthat of any other substance, component 2-c (SF) was second and followed by 2-c., 4-dB,?d2, and di in this order, (5) cholesterol of ester type was present in all the components,except component 2-c. and its subfraction. The presence of cholesterol of free type waslimited to component 4-d2. The ratio of cholesterol ester to total cholesterol in thiscomponent was 50 percent.As is evident from the results mentioned above, all the transaminases separatedfrom adult chicken oxyhemoglobitt required a disc electrophoretic behavior entirely differ-?ent from that of the same transaminases obtained from fowl blood plasma by theauthor2830=3l) in his physicochemical study, and were characterized by the lteme enzyme?5?"). Especially in reversible GPT and some of the CRT-ases, the CRT-ase likereaction of the former, and the possibility of dissociation from CRT-ase to its subunitof the latter were important points of consideration in this report. Furthermore, theabsence of F-GPT isolated was a feature common to the experimental results obtainedfrom adult chicken oxyhemoglobin and its blood plasma30). However, within the scope?of the authors determination of adult chicken oxyhemoglobin, no properties were commonto those enzymes of blood plasma.Therefore, it seemed quite all right to consider that all the transaminases, exceptreversible GPT, appeared to be their isozymes, as compared with the same transaminasesseparated from fowl blood plasma. There can be no practical difficulty in distinguishingisozymes in oxyhemoglobin from those in blood plasma.The transaminase activity values in hemolyzing blood plasma were raised9), probablybecause they reacted in concert with those isozymes.
社団法人日本獣医学会の論文
1973-12-25

鶏 Oxyhemoglobin 中から単離した Aspartate-および Alanine-aminotransferase 系アミノ基転移酵素の活性とその物理化学的性状について

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