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Iron succinyl-protein complex

A brief report describes 3 patients taking cimetidine 1 g and ferrous sulfate 600 mg daily whose ulcers healed after 2 months, but their anaemia and altered iron metabolism persisted. When the cimetidine was reduced to 400 mg daily, but with the same dose of iron, the blood picture resolved satisfactorily within a month. The author of the report attributed this response to the cimetidine-induced rise in gastric pH, which reduced the absorption of the iron. However, this suggested mechanism was subsequently disputed, as medicinal iron is already in the most absorbable form, Fe, and so does not need an acidic environment to aid absorption. A study in patients with iron deficiency, or iron-deficiency anaemia, found that the eoneurrent use of famotidine, nizatidine, or ranitidine, did not affeet their response to 2.4 g of iron succinyl-protein complex (equivalent to 60 mg of iron twice daily). No special precautions would seem necessary on concurrent use. [Pg.1263]

Fig. 17. Spectral shifts of iron complexes caused by succinylating ovotransferrin to varying degrees. The protein was succinylated in the iron-free state. Following dialysis and lyophilization, the modified transferrins were redissolved and saturated with iron, and the visible spectrum was scanned with a Beckman DB recording spectrophotometer. ------, original ovotransferrin (Xmax 465 mg) ---------, succiny-... Fig. 17. Spectral shifts of iron complexes caused by succinylating ovotransferrin to varying degrees. The protein was succinylated in the iron-free state. Following dialysis and lyophilization, the modified transferrins were redissolved and saturated with iron, and the visible spectrum was scanned with a Beckman DB recording spectrophotometer. ------, original ovotransferrin (Xmax 465 mg) ---------, succiny-...
Fig. 18. Effects of acetylation or succinylation of iron ovotransferrin on stabilities of complexes in urea. Acetylated was40% modified succinylated was60—70% modified. General conditions are described in text. Reactions were performed withh 0.5% protein in 0.005 m NaHCOs, 0.001 m sodium citrate, 0.001 m FeNH4(S04)2 at pH 8.4, and 0—8 m urea. Optical densities were determined at 470 mp A — A. unmodified (control) iron ovotransferrin in 0—8 m urea for 1 hour —, acetylated or succinylated ovotransferrin in 0—8 m urea immediately after mixing (zero time) O—O. acetylated or succinylated ovotransferrin in 0—8 m urea for 1 hour. (Biochemistry 4, 998 [1965]). Fig. 18. Effects of acetylation or succinylation of iron ovotransferrin on stabilities of complexes in urea. Acetylated was40% modified succinylated was60—70% modified. General conditions are described in text. Reactions were performed withh 0.5% protein in 0.005 m NaHCOs, 0.001 m sodium citrate, 0.001 m FeNH4(S04)2 at pH 8.4, and 0—8 m urea. Optical densities were determined at 470 mp A — A. unmodified (control) iron ovotransferrin in 0—8 m urea for 1 hour —, acetylated or succinylated ovotransferrin in 0—8 m urea immediately after mixing (zero time) O—O. acetylated or succinylated ovotransferrin in 0—8 m urea for 1 hour. (Biochemistry 4, 998 [1965]).

See other pages where Iron succinyl-protein complex is mentioned: [Pg.117]    [Pg.189]    [Pg.1914]    [Pg.159]    [Pg.781]    [Pg.286]   


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Complex proteins

Iron protein proteins

Protein complexity

Protein succinylation

Proteins complexation

Proteins succinylated

Succinyl

Succinylation

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