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J. Biochem, 1984, Vol. 96, No. 4 1273-1281
© 1984 Japanese Biochemical Society


research-article

Differences between Homogeneous Spermidine Synthases Isolated from Rat and Pig Liver1

Banri YAMANOHA*, Keijiro SAMEJIMA*,2, Terumi NAKAJIMA** and Tadashi YASUHARA**

*Tokyo Biochemical Research Institute Takada, Toshima-ku, Tokyo 171
**Institute for Medical and Dental Engineering, Tokyo Medical and Dental University Kandasurugadai, Chiyoda-ku, Tokyo 101

Spermidine synthase was purified to homogeneity from rat and pig liver by a method modified from a previously reported one using DEAE-Sepharose, S-adenosyl(5')-3-thiopropylamine-Sepharose affinity chromatography, Sephacryl S-300 gel filtration and polyacrylamide gel electrophoresis. No apparent difference between the two enzymes was observed in specific activity, molecular weight (74,000), or subunit composition (two subunits). However, significant differences were observed in their pI values, which were 5.16 for the pig enzyme and 5.34 for the rat enzyme, and their peptide maps. Amino acid compositions of the two enzymes were closely related, but differed significantly in some amino acids. In addition, the rat enzyme was more sensitive to inhibition by S-adenosyl-1, 8-diamino-3-thiooctane than the pig enzyme.

2Present address: Department of Analytical Chemistry, Faculty of Pharmaceutical Sciences, Josai University, Keyakidai, Sakado-shi, Saitama 350–02. To whom correspondence should be addressed.

1This work was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.


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