Abstract
Formation of covalent, higher molecular weight transformation (HMWT) products during storage of insulin preparations at 4-45 degrees C was studied by size exclusion chromatography. The main products are covalent insulin dimers (CID), but in protamine-containing preparations the concurrent formation of covalent insulin-protamine (CIP) products takes place. At temperatures greater than or equal to 25 degrees C parallel or consecutive formation of covalent oligo- and polymers can also be observed. Rate of HMWT is only slightly influenced by species of insulin but varies with composition and formulation, and for isophane (NPH) preparations, also with the strength of preparation. Temperature has a pronounced effect on CID, CIP, and, especially, covalent oligo- and polymer formation. The CIDs are apparently formed between molecules within the hexameric unit common for all types of preparations and rate of formation is generally faster in glycerol-containing preparations. Compared with insulin hydrolysis reactions (see the preceding paper), HMWT is one order of magnitude slower, except for NPH preparations.
MeSH Terms
Chemistry, Pharmaceutical
Chromatography, Gel
Drug Stability
Drug Storage
Insulin/chemistry
Molecular Weight
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Brange J
Novo Research Institute, Bagsvaerd, Denmark.
Havelund S
Hougaard P
References (15)
15 references, click to expand
-
Frequency and specificity of protamine antibodies in diabetic and control subjects.
Diabetes. 1988 Feb;37(2):172-6
PMID: 3292313
-
Chemical stability of insulin. 1. Hydrolytic degradation during storage of pharmaceutical preparations.
Pharm Res. 1992 Jun;9(6):715-26
PMID: 1409351
-
Persistent cutaneous insulin allergy resulting from high-molecular-weight insulin aggregates.
Diabetes. 1990 Jun;39(6):728-33
PMID: 2189764
-
The source of the circulating aggregate of insulin in type I diabetic patients is therapeutic insulin.
J Clin Invest. 1986 Mar;77(3):717-23
PMID: 3512601
-
Phenol stabilizes more helix in a new symmetrical zinc insulin hexamer.
Nature. 1989 Apr 13;338(6216):594-6
PMID: 2648161
-
Proinsulin and the biosynthesis of insulin.
N Engl J Med. 1969 May 15;280(20):1106-13
PMID: 4305118
-
The structure of 2Zn pig insulin crystals at 1.5 A resolution.
Philos Trans R Soc Lond B Biol Sci. 1988 Jul 6;319(1195):369-456
PMID: 2905485
-
Increased thermal stability of proteins in the presence of sugars and polyols.
Biochemistry. 1979 Nov 13;18(23):5191-6
PMID: 497177
-
Chemical modification and cross-linking of proteins by impurities in glycerol.
Arch Biochem Biophys. 1976 Feb;172(2):608-10
PMID: 1259423
-
Reaction of glycolaldehyde with proteins: latent crosslinking potential of alpha-hydroxyaldehydes.
Proc Natl Acad Sci U S A. 1983 Jun;80(12):3590-4
PMID: 6574500
-
Monomeric insulins and their experimental and clinical implications.
Diabetes Care. 1990 Sep;13(9):923-54
PMID: 2226110
-
Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures.
Biochemistry. 1981 Aug 4;20(16):4667-76
PMID: 7295639
-
Isolation and properties of proinsulin, intermediate forms, and other minor components from crystalline bovine insulin.
Diabetes. 1968 Dec;17(12):725-36
PMID: 5726253
-
Antibodies to covalent aggregates of insulin in blood of insulin-using diabetic patients.
Diabetes. 1987 Jul;36(7):838-41
PMID: 2438179
-
Stability of protein pharmaceuticals.
Pharm Res. 1989 Nov;6(11):903-18
PMID: 2687836