鶏血漿中 Albumin 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
書誌事項
- タイトル別名
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- ASPARTATE-AND ALANINE-AMINOTRANSFERASE ACTIVITIES AND PHYSICOCHEMICAL PROPERTIES OF ALBUMIN COMPONENTS SUBFRACTIONATED FROM FOWL BLOOD PLASMA
- ケイ ケッショウ チュウ Albumin カラ タンリ シタ Aspartate- オヨビ Alanine-aminotransferaseケイ アミノキ テンイ コウソ ノ カッセイ ト ソノ モノ リカガクテキ セイジョウ ニ ツイテ
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In view of the results of experirnents34 36) conducted to fractionate the transaminasesin fowl blood plasma, some of these enzymes called forward (F)-aspartate aminotransferase(GOT), reverse (R)-GOT, F-alanine aminotransferase (GPT), and R-GPT were presumedto be contained in a limited number of albumin components35?36). No effective verifi-cation of this conjecture, however, could be made for lack of detailed information on anysystematic method for the subfractionation of fowl blood plasma albumin. Naturally, the physiochemical properties of those enzymes have been left unknown due to insuf-ftcient data.In the present investigation, a practical solution was reached for these problems bymeans of the authors method introduced. This report gives an outline of the methodused for subfractionation of plasma albumin. The results obtained are summarized asfollows. l. Disc electrophoretic analysis revealed tlaat plasma albumin consisted of six differ-ent components classified into four large divisions. The components were called I-a, [-b., I-b., I-(b, c), I-c., and I-c.. Their relative positions are shown in detail in theremarks of Table 3.The major part of the albumin was occupied by two components, I-a and I-(b, c).The ratio of both components to the total albumin was approximately 93%. The yieldper total albumin was maximum.2. The albumins subfractionated were characterized by the following physicochemi-cal properties.(a) Their isoe[ectric points were in a range of pH from 4.4 to 6.0. The isoelectricpoints of components I-a and I-(b, c) were found to be 4.7 and 4.8, respectively.(b) Their sedimentation constants ranged from a minimum value of 4.1 to amaximum value of 4, 9. The sedimentation constants of the two comopnents mentionedabove were found to be 4.4 and 4.6, respectively.(c) The different absorbancy of each component has been interpreted as indicatingthe presence of six different types of conjugated protein. The greater part of each corn-ponent, however, consisted of protein.(d) The albumins were classified roughly into a group of glucoprotein. The con-clusion was indicated by the hexosamine content included in each of the components.3. When the criteria described in Tables 3, 4-A, and 4-B were applied, a more de-tailed classification was made for the transaminases which were usually classified into fourlarge divisions, The classification finally reached is illustrated as follows.On the basis of this classification, the following conclusions could be drawn, (a) The albumin counponents were positiwe for the transamination reaction, as wasexpected. None of them reacted as a self-sttpporting transaminase, as pointecl out fromtlae observation on F-GOT, R-GOT, reversible GOT, and F-GPT mentioned above.(b) The albumin components subfractionated supported all the actixze fragments ofR-GPT.(c) The albumins contained the following transamisases: three isozymes of tlaegrou
収録刊行物
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- 日本獸醫學雜誌(The Japanese Journal of Veterinary Science)
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日本獸醫學雜誌(The Japanese Journal of Veterinary Science) 35 (2), 133-147_1, 1973
公益社団法人 日本獣医学会
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- CRID
- 1390282681401277952
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- NII論文ID
- 110003981174
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- NII書誌ID
- AN00191788
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- COI
- 1:CAS:528:DyaE2cXisFSjtg%3D%3D
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- ISSN
- 18811442
- 00215295
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- NDL書誌ID
- 7616242
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- PubMed
- 4738924
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