Literature DB >> 307603

The equilibrium between metarhodopsin I and metarhodopsin II in the isolated frog retina.

C Baumann.   

Abstract

1. Rapid and slow changes in the absorbance of isolated frog retinae produced by exposure to brief flashes were studied at temperatures between 5 and 30 degrees C.2. Rapid changes observed at 475 nm consist of a transient increase of absorbance followed by an exponential decay to a new level of absorbance which is lower than before the flash exposure.3. The new level of absorbance determines the initial conditions of slow changes following the rapid ones. At higher temperatures, the loss of absorbance during the rapid changes is greater than at lower temperatures. Accordingly, the slow reactions start at lower levels of absorbance when the temperature is high.4. Quantitative analysis showed that the rapid reactions can be described in terms of two consecutive reactions followed by an equilibrium reaction: the light-controlled formation of lumirhodopsin, decay of lumirhodopsin to metarhodopsin I, and the equilibrium reaction between the metarhodopsins I and II.5. The slow absorbance changes observed in the visible (lambda = 480 nm) are due to metarhodopsin I and to metarhodopsin III. Metarhodopsin I decays during the early phase of slow reactions but can noticeably influence the kinetics at lower temperatures.6. The activation energy of the lumirhodopsin decay is 22.5 kcal/mole, that of the conversion of metarhodopsin I into metarhodopsin II is 30.1 kcal/mole. The entropy change associated with the metarhodopsin I-II equilibrium amounts to +34 cal/mole. K.

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Year:  1978        PMID: 307603      PMCID: PMC1282602          DOI: 10.1113/jphysiol.1978.sp012331

Source DB:  PubMed          Journal:  J Physiol        ISSN: 0022-3751            Impact factor:   5.182


  8 in total

1.  The formation of metarhodospin380 in the retinal rods of the frog.

Authors:  C Baumann
Journal:  J Physiol       Date:  1976-07       Impact factor: 5.182

2.  TAUTOMERIC FORMS OF METARHODOPSIN.

Authors:  R G MATTHEWS; R HUBBARD; P K BROWN; G WALD
Journal:  J Gen Physiol       Date:  1963-11       Impact factor: 4.086

3.  The interpretation of spectral sensitivity curves.

Authors:  H J A DARTNALL
Journal:  Br Med Bull       Date:  1953       Impact factor: 4.291

4.  Kinetics of slow thermal reactions during the bleaching of rhodopsin in the perfused frog retina.

Authors:  C Baumann
Journal:  J Physiol       Date:  1972-05       Impact factor: 5.182

5.  Flash photolysis of rhodopsin in the isolated frog retina.

Authors:  C Baumann
Journal:  Vision Res       Date:  1970-09       Impact factor: 1.886

6.  The chemistry of visual photoreception.

Authors:  R Hubbard; D Bownds; T Yoshizawa
Journal:  Cold Spring Harb Symp Quant Biol       Date:  1965

7.  Protein configuration changes in the photolysis of rhodopsin. I. The thermal decay of cattle lumirhodopsin in vitro.

Authors:  F Erhardt; S E Ostroy; E W Abrahamson
Journal:  Biochim Biophys Acta       Date:  1966-02-07

8.  Protein configuration changes in the photolysis of rhodopsin. II. The sequence of intermediates in thermal decay of cattle metarhodopsin in vitro.

Authors:  S E Ostroy; F Erhardt; E W Abrahamson
Journal:  Biochim Biophys Acta       Date:  1966-02-07
  8 in total
  4 in total

1.  A quantitative account of the activation steps involved in phototransduction in amphibian photoreceptors.

Authors:  T D Lamb; E N Pugh
Journal:  J Physiol       Date:  1992-04       Impact factor: 5.182

2.  Temperature dependence of gating current in myelinated nerve fibers.

Authors:  P Jonas
Journal:  J Membr Biol       Date:  1989-12       Impact factor: 1.843

3.  Kinetics and components of the flash photocurrent of isolated retinal rods of the larval salamander, Ambystoma tigrinum.

Authors:  W H Cobbs; E N Pugh
Journal:  J Physiol       Date:  1987-12       Impact factor: 5.182

4.  Effect of pH on the formation and decay of the metarhodopsins of the frog.

Authors:  C Baumann; W Zeppenfeld
Journal:  J Physiol       Date:  1981-08       Impact factor: 5.182

  4 in total

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