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Enzymaktivitäten im Fettgewebe

Enzyme activities in adipose tissue comparison in the rat, swine and man

Vergleichende Untersuchungen bei Ratte, Schwein und Mensch

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Summary

Enzyme patterns (Glucose-6-Phosphatdehydrogenase (EC 1.1.1.49), 6-Phosphogluconatdehydrogenase (EC 1.1.1.44), Hexokinase (EC 2.7.1.1), Phosphofructokinase (EC 2.7.1.11), Pyruvatkinase (EC 2.7.1.40), Glucophosphomutase (EC 2.7.5.1), Glycerin-3-Phosphatdehydrogenase (EC 1.1.1.8), Malatdehydrogenase (EC 1.1.1.37), Glutamatpyruvattransaminase (EC 2.6.1.2), Glutamatoxalacetattransaminase (EC 2.6.1.1), Glutamatdehydrogenase (EC 1.4.1.3), Citrate Cleavage Enzyme (EC 4.1.3.8), Malic Enzyme (EC 1.1.1.38), Glycerokinase (EC 2.7.1.30), Glucose-6-Phosphatase (EC 3.1.3.9) and Fructose-1,6-Diphosphatase (EC 3.1.3.11)) have been measured in subcutaneous adipose tissue of man and pig and in the epididymal fat pads of rats. The conduct of soluble extract-protein was equal in rat (21.7±1.6 mg/g) and man (21.0±1.9 mg/g) but different in pig (5.4±0.5 mg/g). In all three species the pattern was nearly the same; phosphofructokinase was the rate-limiting enzyme of glycolysis; most of the glucose degradation in white adipose tissue seems to be done via the pentose-phosphate-shunt; there was no measurable activity of glycerokinase. In human adipose tissue—where nearly all enzyme activities were about ten times lower—there was no citrate cleavage enzyme either.

Zusammenfassung

Im subcutanen Fettgewebe von Mensch und Schwein sowie im epididymalen Fettgewebe der Ratte wurden Enzymmuster bestimmt: Glucose-6-Phosphatdehydrogenase (EC 1.1.1.49), 6-Phosphogluconatdehydrogenase (EC 1.1.1.44), Hexokinase (EC 2.7.1.1), Phosphofructokinase (EC 2.7.1.11), Pyruvatkinase (EC 2.7.1.40), Glucophosphomutase (EC 2.7.5.1), Glycerin-3-Phosphatdehydrogenase (EC 1.1.1.8), Malatdehydrogenase (EC 1.1.1.37), Glutamatpyruvattransaminase (EC 2.6.1.2), Glutamatoxalacetattransaminase (EC 2.6.1.1), Glutamatdehydrogenase (EC 1.4.1.3), Citrate Cleavage Enzyme (EC 4.1.3.8), Malic Enzyme (EC 1.1.1.38), Glycerokinase (EC 2.7.1.30), Glucose-6-Phosphatase (EC 3.1.3.9) und Fructose-1,6-Diphosphatase (EC 3.1.3.11).

Trotz der unterschiedlichen Lokalisation der Gewebe und des verschiedenen Gehaltes an löslichem Extraktprotein (Ratte:Mensch:Schwein=21,7±1,6:21,0±1,9:5,4±0,5mg/g Frischgewicht) finden sich annähernd übereinstimmende Enzymaktivitätsmuster. Bei allen drei Species ist die Phosphofructokinase das limitierende Glykolyse-Enzym und erfolgt der Glucoseabbau offensichtlich überwiegend über den Pentose-Phosphat-Shunt; eine weitere Gemeinsamkeit ist das Fehlen von Glycerokinase-Aktivität. Bezogen auf Extraktprotein liegen jedoch fast alle Enzymaktivitäten im menschlichen Fettgewebe um annähernd eine Zehnerpotenz niedriger als bei Ratte und Schwein. Im Gegensatz zu diesen beiden Species ist im Humanfettgewebe kein Citrate-Cleavage-Enzyme nachweisbar.

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Authors and Affiliations

  1. I. Medizinische Klinik der Universität München, Germany

    P. Schwandt, H. W. Doerr & W. Krone

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  1. P. Schwandt
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  2. H. W. Doerr
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  3. W. Krone
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Herrn Prof. Dr. H. Schwiegk zum 65. Geburtstag gewidmet.

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Schwandt, P., Doerr, H.W. & Krone, W. Enzymaktivitäten im Fettgewebe. Klin Wochenschr 49, 358–360 (1971). https://doi.org/10.1007/BF01496458

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