Skip to main content
Log in

Bedeutung und Herkunft der Enzyme im Glaskörper des Rindes

Possible significance and origin of enzymes in the vitreous body of cattle

  • Published:
Albrecht von Graefes Archiv für klinische und experimentelle Ophthalmologie Aims and scope Submit manuscript

Summary

The presence of malatedehydrogenase, alkal. phosphatase, GOT- and GPT-aminotransferases and of all glycolytic enzymes in the vitreous body of cattle was demonstrated. As the enzyme patterns of vitreous body and its cells show remarkable similarity, the serum pattern differing significantly, the cortex cells presumably represent the origin of the enzymatically active soluble proteins in the vitreous. Enzyme distribution in vitreous shows the same features as in other connective tissues thus indicating its mesenchymal nature. The “phospho-triose-glycerate-group” of enzymes has been found in the same constant proportions as in other tissues. The activities of its extracellular enzymes could be sufficient to account for the minimal metabolic requirements of the vitreous.

Zusammenfassung

Im Glaskörper des Rindes wurden sämtliche Enzyme der Glykolyse, Malatdehydrogenase, die Transaminasen GOT und GPT sowie alkal. Phosphatase nachgewiesen. Die Enzymmuster des Glaskörpers und seiner Zellen entsprechen einander, während die Verteilung im Serum deutlich abweicht, weshalb die Hyalocyten als hauptsächlicher Ursprungsort für die enzymatisch aktiven löslichen Proteine des Glaskörpers angenommen werden. Die Ähnlichkeit des Enzymmusters mit anderen Bindegeweben unterstreicht die mesenchymale Natur des Glaskörpers. Wie alle bisher untersuchten Gewebearten weist auch Glaskörper konstante Proportionen der Enzyme der „Phospho-Triose-Glycerat-Gruppe“ auf. Die Aktivität der extracellulären Enzyme könnte ausreichen, um den minimalen Stoffwechsel des Glaskörpers zu bewerkstelligen.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

Literatur

  • Agarwal, L. P., Brar, G., Goswamy, S.: Phosphatases in rabbit vitreous body. Orient. Arch. Ophthal. 7, 158–162 (1969)

    Google Scholar 

  • Balazs, E.A.: Physiology of the vitreous body. In: Importance of the vitreous body in retina surgery, p. 35 (Schepens C. L. ed.). St. Louis: Mosby 1960

    Google Scholar 

  • Balazs, E. A., Toth, L. Z. J., Eckl, E. A., Mitchell, A. P.: Studies on the structure of the vitreous body XII. Cytological and histochemical studies on the cortical tissue layer. Exp. Eye Ees. 3, 57–71 (1964)

    Google Scholar 

  • Bastide, P.: Activités enzymatiques dans l'humeur aqueuse et le corps vitré. Biol. et Méd. 51, 386–427 (1962)

    Google Scholar 

  • Bay, M.: Comparison between two methods of removing the vitreous body. Acta ophthal. (Kbh.) 50, 166–173 (1972)

    Google Scholar 

  • Bergmeyer, H. U.: Methoden der enzymatischen Analyse I, 378ff, LDH: S. 533. Weinheim: Verlag Chemie 1970

    Google Scholar 

  • Berman, E. R., Gombos, G. M.: Studies on the incorporation of U-14C-Glucose into vitreous polymers in vitro and in vivo. Invest. Ophthal. 8, 521–534 (1969)

    Google Scholar 

  • Berman, E. R., Michaelson, I. C.: The chemical composition of the human vitreous body as related to age and myopia. Exp. Eye Res. 3, 9–15 (1964)

    Google Scholar 

  • Brückner, R.: Auge und Cholinesterase. Ophthalmologica (Basel) 105, 37–49 (1943)

    Google Scholar 

  • Cernea, P., Herscovici, J., Ursu, N.: Determinations of enzymes in the aqueous humor and vitreous body. Oftalmologia 14, 137–146 (1970)

    Google Scholar 

  • Crabtree, B., Newsholme, E. A.: The activities of phosphorylase, hexokinase, phosphofructokinase, lactate dehydrogenase and the glycerol 3-phosphate dehydrogenases in muscles from vertebrates and invertebrates. Biochem J. 126, 49–58 (1972)

    Google Scholar 

  • Delbrück, A.: Untersuchungen über Enzyme des Energie-Stoffwechsels im Bindegewebe. Klin. Wschr. 40, 677–684 (1962)

    Google Scholar 

  • Delbrück, A.: Enzymverteilungsmuster gefäßloser Gewebe. Klin. Wschr. 41, 488–493 (1963)

    Google Scholar 

  • Dische, Z.: Biochemistry of connective tissue of the vertebrate eye. Int. Rev. Connect. Tissue Res. 5, 209–274 (1970)

    Google Scholar 

  • Duke-Elder, S., Cook, C.: System of Ophthalmology, Vol. III, Pt. 1, Embryology. London: Henri Kimpton 1963

    Google Scholar 

  • Duve, C. de: Is there a glycolytic particle ? Wenner-Gren Symposium on structure and function of oxidation-reduction enzymes, p. 715–28 (A. Akeson, A. Ehrenberg, eds.). Oxford: Pergamon Press 1972

    Google Scholar 

  • Eyring, E. J., Anderson, C. E., Ludowieg, J.: Phosphate transfer enzymes incartilage. Arthr. and Rheum. 6, 208–215 (1963)

    Google Scholar 

  • Feissli, S., Forster, G., Laudahn, G., Schmidt, E., Schmidt, F. W.: Normal-Werte und Alterung von Hauptkettenenzymen im Serum. Klin. Wschr. 44, 390–396 (1966)

    Google Scholar 

  • Francois, J., Victoria-Troncoso, V.: Transplantation of vitreous cell culture. Ophthal. Res. 4, 270–280 (1972/73)

    Google Scholar 

  • Francois, J., Victoria-Troncoso, V.: Les facteurs biologiques dans la chirurgie du corps vitré. Ophthalmologica (Basel) 166, 372–398 (1973)

    Google Scholar 

  • Freeman, M. J., Jacobson, B., Toth, L. Z., Balazs, E. A.: Lysosomal enzymes associated with vitreous hyalocyte granules, 1. Intracellular distribution pattern of enzymes. Exp. Eye Res. 7, 113–120 (1968)

    Google Scholar 

  • Friedburg, D.: Enzymverteilungsmuster in der Linse. Ber. dtsch. ophthal. Ges. 69, 446–451 (1969)

    Google Scholar 

  • Gärtner, J.: The fine structure of the vitreous base of the human eye and pathogenesis of pars planitis. Amer. J. Ophthal. 71, 1317–1327 (1971)

    Google Scholar 

  • Geigy, AG: Wissenschaftliche Tabellen, S. 581. Basel: 1969

  • Gloor, B. P.: Zur Entwicklung des Glaskörpers und der Zonula. II. Glaskörperzellen während Entwicklung und Rückbildung der Vasa hyaloidea und der Tunica vasculosa lentis. Albrecht v. Graefes Arch. klin. exp. Ophthal. 186, 311–328 (1973a)

    Google Scholar 

  • Gloor, B. P.: Zur Entwicklung des Glaskörpers und der Zonula. III. Herkunft. Lebenszeit und Ersatz der Glaskörperzellen beim Kaninehen. (Autoradiographische Untersuchungen mit 3H-Thymidin). Albrecht v. Graefes Arch. klin. exp. Ophthal. 187, 21–44 (1973b)

    Google Scholar 

  • Gloster, J.: Carbonic anhydrase in the vitreous body. Brit. J. Ophthal. 40, 487–491 (1956)

    Google Scholar 

  • Greiling, H., Kisters, R., Engels, G.: Die Enzyme in der Synovialflüssigkeit und ihre pathologische Bedeutung. Enzymologia 30, 135–146 (1966)

    Google Scholar 

  • Hoffmann, K., Wurster, U.: Isoenzyme der Lactatdehydrogenase im Glaskörper des Rindes. Vergleich mit anderen Augenabschnitten und Serum. Albrecht v. Graefes Arch. klin. exp. Ophthal. 189, 309–321 (1974)

    Google Scholar 

  • Kasavina, B. S., Chesnokova, N. B.: Lysosomal hydrolases of the eye tissues and the effect of corticosteroids on their activity. Exp. Eye Res. 16, 227–233 (1973)

    Google Scholar 

  • Keller, P.: Serumenzyme beim Rind: Organanalysen und Normalwerte. Schweiz. Arch. Tierheilk. 113, 615–626 (1971)

    Google Scholar 

  • Laurent, T. C.: Enzyme reactions in polymer media. Eur. J. Biochem. 21, 498–506 (1971)

    Google Scholar 

  • Laurent, U. B. G., Laurent, T. C., Howe, A. F.: Chromatography of soluble proteins from the bovine vitreous body on DEAE cellulose. Exp. Eye Res. 1, 276–285 (1962)

    Google Scholar 

  • Lowry, H., Rosebrough, N. J., Farr, A. U., Randall, R. J.: Protein measurement with the folin phenol reagent. J. biol. Chem. 193, 265–275 (1951)

    Google Scholar 

  • Mandel, P., Klethi, J.: Répartition des nucléotides libres dans les diverses zones du cristallin de veau. Biochim. biophys. Acta. (Amst.) 28, 199–200 (1958)

    Google Scholar 

  • Marquardt, P., Süllman, H.: Fermente des Auges. Tabul. biol. 22, P 2, 143–172 (1951)

    Google Scholar 

  • Maurice, D. M.: Protein dynamics in the eye studied with labelled proteins. Amer. J. Ophthal. 47, 361–68 (1959)

    Google Scholar 

  • Merten, R., Solbach, H. G.: Enzymverteilungsmuster des glykolytischen Systems und Citronensäurecyclus im Plasma Krebskranker. Klin. Wschr. 39, 222–232 (1961)

    Google Scholar 

  • Österlin, S. E.: The synthesis of hyaluronic acid in the vitreous III. In vivo metabolism in the owl monkey. Exp. Eye Res. 7, 524–533 (1968c)

    Google Scholar 

  • Österlin, S. E.: The synthesis of hyaluronic acid in the vitreous IV. Regeneration in the owl monkey. Exp. Eye Res. 8, 27–34 (1969)

    Google Scholar 

  • Österlin, S. E., Jacobson, B.: The synthesis of hyaluronic acid in vitreous I. Soluble and particulate transferases in hyalocytes. Exp. Eye Res. 7, 497–510 (1968a)

    Google Scholar 

  • Österlin, S. E., Jacobson, B.: The synthesis of hyaluronic acid in vitreous II. The presence of soluble transferase and nucleotide sugar in the acellular vitreous gel. Exp. Eye Res. 7, 511–523 (1968b)

    Google Scholar 

  • Pau, H.: Die Neubildung des Glaskörpers und seiner Fibrillen. Albrecht v. Graefes Arch. klin. exp. Ophthal. 168, 521–528 (1965)

    Google Scholar 

  • Pette, D.: Plan und Muster im zellulären Stoffwechsel. Naturwissenschaften 52, 597–616 (1965)

    Google Scholar 

  • Pette, D., Luh, W., Bücher, Th.: A constant-proportion group in the enzyme activity pattern of the Embden-Meyerhof chain. Biochem. biophys. Res. Commun. 7, 419–424 (1962)

    Google Scholar 

  • Schmidt, E., Schmidt, F. W.: Enzymmuster menschlicher Gewebe. Klin. Wschr. 38, 957–962 (1960)

    Google Scholar 

  • Shakespeare, P., Ellis, R. B., Mayer, R. J., Hübscher, G.: Glucose metabolism in the mucosa of the small intestine. Enzymes of the glycolytic pathway. Int J. Biochem. 3, 671–676 (1972)

    Google Scholar 

  • Shonk, C. E., Boxer, G. E.: Enzyme patterns in human tissues I. Methods for the determination of glycolytic enzymes. Cancer Res. 24, 709–721 (1964)

    Google Scholar 

  • Smith, J. W., Serafini-Fracassini, A.: The relationship of hyaluronate and collagen in the bovine vitreous body. J. Anat. (Lond.) 101, 99–112 (1967)

    Google Scholar 

  • Swann, D. A., Constable, I. J.: Vitreous structure I. Distribution of hyaluronate and protein. Invest. Ophthal. 11, 159–163 (1972a)

    Google Scholar 

  • Swann, D. A., Constable, I. J.: Vitreous structure II. Role of hyaluronate. Invest. Ophthal. 11, 164–168 (1972b)

    Google Scholar 

  • Vass, Z., Erdei, Z.: Autolytic hydrolysis of the human vitreous body. Acta ophthal. (Kbh.) 45, 677–679 (1967)

    Google Scholar 

  • Vernon-Roberts, B.: The Macrophage. Cambridge: Univ. Press. 1972

    Google Scholar 

  • Witmer, R., Hirsch-Hoffmann, A. M., Speiser, P.: Zur Genese der amotio retinae. Biochemie der retroretinalen Flüssigkeit. Docum. ophthal. (Den Haag) 20, 441–451 (1966)

    Google Scholar 

  • Yamaguchi, T., Hamada, M.: Ontogenetic studies of lactate dehydrogenase isoenzymes in human and chicken eye tissues. Jap. J. Ophthal. 15, 31–40 (1971)

    Google Scholar 

  • Zeller, E. A., Shoch, D.: Über das Vorkommen und die biologische Funktion der Linsenpeptidasen. 18. Int. Kongr. Ophthalmol. Brüssel 1958

Download references

Author information

Authors and Affiliations

Authors

Additional information

Diese Arbeit enthält Ausschnitte der Dissertation von U. E. Wurster.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Hoffmann, K., Wurster, U.E. Bedeutung und Herkunft der Enzyme im Glaskörper des Rindes. Albrecht von Graefes Arch. Klin. Ophthalmol. 190, 79–96 (1974). https://doi.org/10.1007/BF00414338

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00414338

Navigation