Uroporphyrinogen I synthase isoenzymes from bovine and human erythrocytes

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

Research output: Contribution to journalArticlepeer-review

2 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)769-773
Number of pages5
JournalInternational Journal of Biochemistry
Issue number5-6
StatePublished - 1980


Dive into the research topics of 'Uroporphyrinogen I synthase isoenzymes from bovine and human erythrocytes'. Together they form a unique fingerprint.

Cite this