Biochemical aspects of the visual process. XXII. Amino group modification in bovine rod photoreceptor membranes.
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[1] A. Glazer,et al. Chemical modification of proteins: Selected methods and analytical procedures , 1975 .
[2] E A Dratz,et al. Where is rhodopsin? , 1973, Nature: New biology.
[3] W. D. de Grip,et al. The binding site of retinaldehyde in cattle rhodopsin. , 1973, Biochimica et biophysica acta.
[4] G. Falk,et al. An analysis of light‐induced admittance changes in rod outer segments , 1973, The Journal of physiology.
[5] V. Tomasi,et al. The role of phosphatidylserine in the hormonal control of adenylate cyclase of rat liver plasma membranes. , 1972, Biochimica et biophysica acta.
[6] M. Reporter,et al. Methylation of bovine rhodopsin. , 1972, Nature: New biology.
[7] A. M. Cook,et al. Effect of phosphatidyl serine decarboxylase on neural excitation. , 1972, Nature: New biology.
[8] W. D. de Grip,et al. Enrichment of rhodopsin in rod outer segment membrane preparations. Biochemical aspects of the visual process. 18. , 1972, Vision research.
[9] W. D. de Grip,et al. Biochemical aspects of the visual process. XX. The molecular weight of rhodopsin. , 1972, Biochimica et biophysica acta.
[10] F. Daemen,et al. Removal of amino group containing phospholipids from rhodopsin. XVII. Biochemical aspects of the visual process. , 1972, Archives of biochemistry and biophysics.
[11] R. Fager,et al. Aqueous cyanohydridoborate reduction of the rhodopsin chromophore. , 1972, Biochemical and biophysical research communications.
[12] P. K. Brown. Rhodopsin rotates in the visual receptor membrane. , 1972, Nature: New biology.
[13] R. Cone. Rotational diffusion of rhodopsin in the visual receptor membrane. , 1972, Nature: New biology.
[14] J. Rotmans,et al. On the chromophoric group of rhodopsin. , 1972, Vision research.
[15] W. Robinson,et al. Molecular weight of frog rhodopsin. , 1972, Nature: New biology.
[16] H. Heitzmann. Rhodopsin is the predominant protein of rod outer segment membranes. , 1972, Nature: New biology.
[17] M. Zorn. The reduction of rhodopsin with sodium borohydride under non-bleaching conditions. , 1971, Biochimica et biophysica acta.
[18] J. Rotmans,et al. Biochemical aspects of the visual process. 13. The role of phospholipids in cattle rhodopsin studied with phospholipase C. , 1971, Archives of biochemistry and biophysics.
[19] F. Daemen,et al. Biochemical aspects of the visual process. XIV. The binding site of retinaldehyde in rhodopsin studied with model aldimines. , 1971, Archives of biochemistry and biophysics.
[20] T. Richardson,et al. Dansylation of casein micelles and purified fractions. Functional group analysis and effect on micelle formation , 1971 .
[21] D. Gill,et al. Resonance-enhanced Raman spectra of visual pigments in intact bovine retinas at low temperatures. , 1970, Biochemical and biophysical research communications.
[22] S. Knutton,et al. A structural study of the modification of erythrocyte ghosts by phospholipase C. , 1970, Biochimica et biophysica acta.
[23] J. De Pont,et al. Biochemical aspects of the visual process. 8. Enzymatic conversion of retinylidene imines by retinoldehydrogenase from rod outer segments. , 1970, Archives of biochemistry and biophysics.
[24] J. De Pont,et al. Biochemical aspects of the visual process. VII. Equilibrium conditions in the formation of retinylidene imines. , 1970, Archives of biochemistry and biophysics.
[25] R. E. Anderson,et al. Phospholipids of bovine outer segments. , 1970, Biochemistry.
[26] S. Fleischer,et al. Lipid composition of bovine retinal outer segment fragments. , 1970, Biochimica et biophysica acta.
[27] F. Daemen,et al. Biochemical aspects of the visual process. VI. The lipid composition of native and hexane-extracted cattle rod outer segments. , 1970, Biochimica et biophysica acta.
[28] R. P. Poincelot,et al. Fatty acid composition of bovine rod outer segments and rhodopsin. , 1970, Biochimica et biophysica acta.
[29] J. Heller,et al. Structure of the glycopeptide from bovine visual pigment 500. , 1970, Biochemistry.
[30] R. Whittam,et al. ATPase Activity of the Sodium Pump needs Phosphatidylserine , 1970, Nature.
[31] R. Hubbard. Absorption Spectrum of Rhodopsin: 500 nm Absorption Band , 1969, Nature.
[32] J. Heller. Structure of visual pigments. I. Purification, molecular weight, and composition of bovine visual pigment500. , 1968, Biochemistry.
[33] N. Seiler,et al. Quantitative Bestimmung von Aminen und von Aminosäuren als 1-Dimethylamino-naphthalin-5-sulfonsÄureamide auf Dünnschichtchromatogrammen , 1966 .
[34] A. Habeeb,et al. Determination of free amino groups in proteins by trinitrobenzenesulfonic acid. , 1966, Analytical biochemistry.
[35] S. Futterman. Metabolism of the retina. III. The role of reduced triphoshopyridine nucleotide in the visual cycle. , 1963, The Journal of biological chemistry.
[36] M. Ludwig,et al. The Reaction of Imidoesters with Proteins and Related Small Molecules , 1962 .
[37] Tetsuya Komori,et al. Chemische Studien uber die visuelle Funktion. VIII. Uber den Aminosaure-Bestandteil und die N-terminale Aminosaure von Kroten-Scotopsin. , 1961 .
[38] S. Futterman,et al. The estimation of vitamin A aldehyde with thiobabituric acid. , 1961, The Journal of biological chemistry.
[39] G. Albrecht. Terminal amino acids of rhodopsin. , 1957, The Journal of biological chemistry.
[40] G. Wald,et al. CIS-TRANS ISOMERS OF VITAMIN A AND RETINENE IN THE RHODOPSIN SYSTEM , 1952, The Journal of general physiology.