Catalyst – solid sorbent – or support therefor: product or process – Solid sorbent – Organic
Patent
1995-12-06
1998-10-13
Caldarola, Glenn
Catalyst, solid sorbent, or support therefor: product or process
Solid sorbent
Organic
502402, 502403, 502400, 210656, 210692, 210690, 435180, 435182, 530413, 530415, B01J 2000, C12N 1106, A23J 100
Patent
active
058211934
DESCRIPTION:
BRIEF SUMMARY
TECHNICAL FIELD
The present invention relates to an adsorbent for removing ketoamine-containing protein, more particularly, it relates to an adsorbent for removing ketoamine-containing protein in body fluid, a process for removing ketoamine-containing protein by using the above-mentioned adsorbent, a process preventing or treating for diabetic complications by removing ketoamine-containing protein with the adsorbent and an adsorber for ketoamine-containing protein.
BACKGROUND ART
After a few years have passed since a patient exhibits the onset of diabetes, in most of all the cases, a pathologic change in kidney glomerula appears. Most of the causes of death of diabetics also are due to nephropathy, and recently, a ratio of a patient with renal insufficiency which is caused due to diabetic nephropathy has been increasing. This is due to angiopathy occured in kidney glomerula (ref. Diabetes and Renovascular Arteria, PRACTICE, 3, 298 (1986) and Relationship between Diabetes and Blood Vessel, The Bulletin of the Japan Diabetes Society General Meeting, 1 (1988)).
Although there is present a large amount of sugar present in the blood of a diabetic, compared to a normal adult, it is known that glucose which is present in blood bonds to protein and the like without participation of an enzyme. Protein binds to sugar nonenzymatically to form ketoamine-containing protein, then, the ketoamine-containing protein deposits on the vessel wall, and, as a result, causes angiopathy. This leads to serious diabetic complications. Also, a substance which is obtained by a reaction between ketoamine-containing protein is formed. These are known as Advanced Glycosylation End Products (AGEs). AGEs are substances wherein glycosylated proteins are cross-linked to each other, and has been considered as a causative substance of diabetic complication (ref. Nonenzymatic Glycosylation and the Pathogenesis of Diabetic Complications; Annals of Internal Medicine, 101, 527 (1984) and Advanced Glycosylation End Products in Patients with Diabetic Nephropathy; The New England Journal of Medicine, 325, 836 (1991)).
Although a treatment for diabetic complication currently depends on a vigorous insulin therapy or a depressor therapy, once clinically apparent nephropathy progresses, it is difficult to halt the progression of the disease. Alternatively, as to non-insulin dependent diabetes mellitus, there is not an effective treatment for the disease at this time.
In the field of food, the fact that sugar adds to protein to give a saccharificated protein, has been known for a long time, and a lot of attempts to inhibit glycation have been carried. For example, in the publications, Japanese Unexamined Patent Publication No. 142114/1987 and Japanese Unexamined Patent Publication No. 156/1990, which were filed with Japanese Patent Office by The Rockefeller University, the fact that addition of a composition containing hydrazine or aminoguanidine to desired protein shows an effect inhibiting glycation of the protein is described. This fact shows that a compound dissolved in an aqueous solution inhibits glycation of protein.
A hydrazide derivative and the like have been employed for carrying a ligand in affinity chromatography for a long time (ref. Experiment and Application, Affinity Chromatography: Kodansha (1976)). For example, there is a method wherein a hydrazide derivative which is carried on a carrier is allowed to react with a compound (ligand) containing a carboxyl group in the presence of carbodiimide, and furthermore, to react with the aldehyde group of ring-cleaved sugar to fix sugar as a ligand. But the hydrazide derivative-carrying carrier has been used as an adsorbent for affinity. A condition which allows the hydrazide derivative-carrying carrier (adsorbent) to react with aldehyde group needs a higher reaction temperature, a longer reaction time and a larger amount of an aldehyde compound and the like in comparison with a condition being used in extracorporeal circulation (ref. Experiment and Application, Affinity Chromatography: 65 to
REFERENCES:
patent: 3947352 (1976-03-01), Cuatrecasas et al.
patent: 4419444 (1983-12-01), Quash
Yoshihei, Diabetes and Renovascular Arteria, Practice, 3, pp. 298-302 (1986).
Relationship between Diabetes and Blood Vessel, The Bulletin of the Japan Diabetes Society General Meeting, 1, pp. 1-5 (1988).
Brownlee et al, Annals of Internal Medicine, 101, pp. 527-537 (1984).
Makita et al, The New England Journal of Medicine, vol. 325, No. 12, pp. 836-842 (1991).
Experiment and Application, Affinity Chromatography, pp. 16-95 Kodansha (1976).
Acharya et al, The Journal of Biological Chemistry, vol. 225, No. 15, pp. 7218-7224 (1980).
Brownlee et al, The New England Journal of Medicine, vol. 318, No. 20, pp. 1315-1321 (1988).
Ogino Eiji
Tani Nobutaka
Bullock In Suk
Caldarola Glenn
Kanegafuchi Kagaku Kogyo & Kabushiki Kaisha
LandOfFree
Adsorbent having a terminal hydrazine group and a method for rem does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Adsorbent having a terminal hydrazine group and a method for rem, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Adsorbent having a terminal hydrazine group and a method for rem will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-313101