Uroporphyrinogen I synthase isoenzymes from bovine and human erythrocytes

K. Miyagi; Z. J. Petryka; M. Kaneshima; J. Kawakami; C. A. Pierach

doi:10.1016/0020-711X(80)90160-3

Uroporphyrinogen I synthase isoenzymes from bovine and human erythrocytes

K. Miyagi, Z. J. Petryka, M. Kaneshima, J. Kawakami, C. A. Pierach

Medicine - Administration

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Abstract

1. 1. Uroporphyrinogen I synthase (UPGI-S) was purified from bovine erythrocytes to 1300 fold and from human to 400 fold. 2. 2. Six UPGI-S isoenzymes were separated from both bovine and human erythrocytes. 3. 3. Stability experiment indicated there were two groups among human UPGI-S isoenzymes: (1) low stability-high activity (S_H1-S_H3) and (2) high stability-low activity (S_H4-S_H6). 4. 4. UPGI-S isoenzymes S_H1, S_H2 and S_H3 were the major portion of total UPGI-S activity for human, while for bovine isoenzymes, S_B4, S_B1 and S_B6 were the major component in the enzyme activity.

Original language	English (US)
Pages (from-to)	769-773
Number of pages	5
Journal	International Journal of Biochemistry
Volume	12
Issue number	5-6
DOIs	https://doi.org/10.1016/0020-711X(80)90160-3
State	Published - 1980

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title = "Uroporphyrinogen I synthase isoenzymes from bovine and human erythrocytes",

abstract = "1. 1. Uroporphyrinogen I synthase (UPGI-S) was purified from bovine erythrocytes to 1300 fold and from human to 400 fold. 2. 2. Six UPGI-S isoenzymes were separated from both bovine and human erythrocytes. 3. 3. Stability experiment indicated there were two groups among human UPGI-S isoenzymes: (1) low stability-high activity (SH1-SH3) and (2) high stability-low activity (SH4-SH6). 4. 4. UPGI-S isoenzymes SH1, SH2 and SH3 were the major portion of total UPGI-S activity for human, while for bovine isoenzymes, SB4, SB1 and SB6 were the major component in the enzyme activity.",

author = "K. Miyagi and Petryka, {Z. J.} and M. Kaneshima and J. Kawakami and Pierach, {C. A.}",

year = "1980",

doi = "10.1016/0020-711X(80)90160-3",

language = "English (US)",

volume = "12",

pages = "769--773",

journal = "International Journal of Biochemistry",

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TY - JOUR

T1 - Uroporphyrinogen I synthase isoenzymes from bovine and human erythrocytes

AU - Miyagi, K.

AU - Petryka, Z. J.

AU - Kaneshima, M.

AU - Kawakami, J.

AU - Pierach, C. A.

PY - 1980

Y1 - 1980

N2 - 1. 1. Uroporphyrinogen I synthase (UPGI-S) was purified from bovine erythrocytes to 1300 fold and from human to 400 fold. 2. 2. Six UPGI-S isoenzymes were separated from both bovine and human erythrocytes. 3. 3. Stability experiment indicated there were two groups among human UPGI-S isoenzymes: (1) low stability-high activity (SH1-SH3) and (2) high stability-low activity (SH4-SH6). 4. 4. UPGI-S isoenzymes SH1, SH2 and SH3 were the major portion of total UPGI-S activity for human, while for bovine isoenzymes, SB4, SB1 and SB6 were the major component in the enzyme activity.

AB - 1. 1. Uroporphyrinogen I synthase (UPGI-S) was purified from bovine erythrocytes to 1300 fold and from human to 400 fold. 2. 2. Six UPGI-S isoenzymes were separated from both bovine and human erythrocytes. 3. 3. Stability experiment indicated there were two groups among human UPGI-S isoenzymes: (1) low stability-high activity (SH1-SH3) and (2) high stability-low activity (SH4-SH6). 4. 4. UPGI-S isoenzymes SH1, SH2 and SH3 were the major portion of total UPGI-S activity for human, while for bovine isoenzymes, SB4, SB1 and SB6 were the major component in the enzyme activity.

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JO - International Journal of Biochemistry

JF - International Journal of Biochemistry

SN - 1357-2725

IS - 5-6

ER -

Uroporphyrinogen I synthase isoenzymes from bovine and human erythrocytes

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