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Similarity and differences in the physicochemical properties of lactate dehydrogenase isozymes from different tissues of Japanese sandfish Arctoscopus japonicus

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  • Chemistry and Biochemistry
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Abstract

Vertebrates have three genes (LDHA, LDHB, and LDHC) encoding skeletal muscle-, heart muscle- and testis-specific lactate dehydrogenase (LDH, E.C. 1.1.1.27), respectively. The muscle and heart LDHs are tetramers formed by polypeptides encoded by LDHA and LDHB, but not LDHC. The catalytic activity and physicochemical characteristics of testis LDH (tLDH) differs from those of the other two isozymes. There have been few kinetic analyses of fish tLDH. Moreover, the mechanism enabling enzymatic activity to be sustained in low temperature-adapted fish remains unclear. In the present study, tLDH and white muscle LDH (mLDH) were isolated from the Japanese sandfish Arctoscopus japonicas, the habitat of which ranges from 1.5 to 13 °C in temperature. The K m and V max of mLDH and tLDH with pyruvate were similar, but their thermostabilities differed. The of K m and V max values increased with increasing temperature between 5 and 40 °C, and the van’t Hoff ΔH values for pyruvate reduction by mLDH and tLDH were 35 and 31 kJ mol−1, respectively. Our findings indicate that LDH function and structure (thermal stability) are highly conserved in skeletal muscle and testis, but unique properties are acquired in each tissue depending on its function.

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Acknowledgments

This work was supported in part by JSPS KAKENHI grant numbers 15K09448 to WN and 15K09516 to HW, and by a private donation from Dr. Ken Satoh, Satoh Naíka Clinic, Sakata 998-0013, Japan.

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Author notes

  1. Kotomi Sugawara

    Present address: Department of Hematology, Nephrology, and Rheumatology, Graduate School of Medicine, Akita University, Akita, 010-8543, Japan

  2. Shigeyoshi Nakamura

    Present address: Kitakyusyu National College of Technology, Fukuoka, 802-0985, Japan

Authors and Affiliations

  1. Department of Life Science, Akita University, Akita, 010-8502, Japan

    Kotomi Sugawara

  2. Department of Life Science, Graduate School of Engineering and Resource Science, Akita University, Akita, 010-8502, Japan

    Mizuki Nakagawa, Mika Yonezawa, Hideki Wakui & Wataru Nunomura

  3. Department of Bioengineering, Graduate School of Engineering, Nagaoka University of Technology, Nagaoka, 940-2188, Japan

    Shigeyoshi Nakamura & Shun-ichi Kidokoro

  4. Research Center for Engineering Science, Graduate School of Engineering and Resource Science, Akita University, Akita, 010-8502, Japan

    Wataru Nunomura

Authors
  1. Kotomi Sugawara
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  2. Mizuki Nakagawa
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Correspondence to Wataru Nunomura.

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Sugawara, K., Nakagawa, M., Yonezawa, M. et al. Similarity and differences in the physicochemical properties of lactate dehydrogenase isozymes from different tissues of Japanese sandfish Arctoscopus japonicus . Fish Sci 82, 519–527 (2016). https://doi.org/10.1007/s12562-016-0972-1

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