Untersuchungen am ribosomalen Ferritin normaler, cirrhotischer und carcinomatöser menschlicher Lebern

α-Helical Structures and Iron Contents of the Ribosomal Ferritin from Normal, Cirrhotic and Cancerous Human Livers

“…The preparation of ribosomes from human liver was performed according to Korner [7], as described in detail previously [2]. In the same study the preparation of ribosomal ferritin by Sepharose-4B chromatography of ribosomes is presented.…”

“…In the same study the preparation of ribosomal ferritin by Sepharose-4B chromatography of ribosomes is presented. The purity of the eluate fractions containing ferritin was checked by treatment with cadmium sulphate [5] yielding crystals with the conformation characteristic of ferritin [2]. Moreover, the ferritin fractions were submitted to disc electrophoresis in polyacrylamide gels and stained for both protein and iron.…”

“…Moreover, the ferritin fractions were submitted to disc electrophoresis in polyacrylamide gels and stained for both protein and iron. As no protein band other than iron-containing protein bands was found, the ferritin being investigated can be considered to be free from contaminating proteins [2], For ORD measurements the iron-free protein fractions of the ribosomal ferritins were used. These apoferrilins were prepared by the sodium dithionite method [4] followed by removal of traces of iron with bipyridyl.…”

“…The iron contents of the ribosomal ferritin as well as of the cytoplasmatically localized ferritin [5,12] from cirrhotic and cancerous human livers are decreased significantly as compared with normal livers. In previous experiments employing polyacryla mide gel electrophoresis, molecular weight determination and amino acid analysis, the ribosomal apoferritins from pathological livers were shown to differ structurally from normal apoferritin [2], Changes in protein structure may be discussed to decrease the capacity of apoferritin for iron uptake. Therefore, the ribosomal apoferritin fractions from normal, cirrhotic and cancerous human livers were submitted to optical rotatory dispersion (ORD) [1,3,6] measurements, in order to obtain informations regarding their con formations, especially their a-helical contents.…”

“…In a previous communication the preparation of a ribosomal chromoproteid fraction from human liver was described [2]. This chromoproteid was characterized as ferritin by its iron contents, absorption spectrum, molecular weight, amino acid composition and crystal shape.…”