Permeability of renal capillaries. I. Preparation of neutral and charged protein probes

Acta Physiologica Scandinavica
G OjtegM Wolgast


This paper describes the preparation of charged and uncharged protein molecular probes for study of the permselectivity of renal capillaries. Horse heart myoglobin was used as a neutral myoglobin. Since it contained several fractions with different isoelectric points, it was purified by fast protein liquid chromatography (FPLC). To obtain a negatively charged myoglobin, the original horse heart myoglobin was treated with cyanate, resulting in net charge of -5.7 +/- 0.3 at physiological pH (mean +/- SEM). The charge was determined from the Donnan potential which develops over a semipermeable membrane separating the inside solution in which the protein was dissolved from a surrounding bath of equal ionic strength. Sperm whale myoglobin was similarly purified by FPLC and used as a positively (+1.7 +/- 0.2) charged isomer. Horseradish peroxidase (HRP) was purified by means of gel and ion-exchange chromatography and found to be neutral at physiological pH. Negatively charged (-14.0 +/- 0.5) HRP was obtained by succinylation. Two isomers of lactate dehyrogenase (LDH) were used, namely the slightly positive (+2) LDH-M4 and the strongly negative (-19) LDH-H4. These isomers, which occur naturally, did not require further purification. T...Continue Reading


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Related Concepts

Vascular Permeability
Molecular Sieve Chromatography
High Pressure Liquid Chromatography Procedure
Iodine Radioisotopes
Isoelectric Focusing
Lactate Dehydrogenase
Protein Conformation

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