Insulin in post-mortem blood

Lindquist, Olle; Rammer, Lennart

doi:10.1007/bf00201181

Cited by 23 publications

(7 citation statements)

References 4 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In post mortem insulin assays the insulin values measured in right heart blood were about ten times higher probably due to post-mortal diffusion of insulin via the portal vein [67,128]. The measurements should therefore be made on peripheral venous (femoral or iliac) blood [25]. Fig.…”

Section: Analytical Interferences and Sample Storage For The Peptidesmentioning

confidence: 98%

“…Using non-compartmental analysis in a case of human insulin intoxication in a type 1 diabetic, Shibutani and Ogawa [23] found an elimination half-life of 6.2 h. In another case of insulin poisoning in a type 1 diabetic patient, Fasching [24] identified a slow biphasic decrease with half-lives of 4 and 10 h for the two successive phases, respectively. Forensic scientists reported that serum insulin concentration in corpses varies significantly amongst individuals [25]. Iwase et al [26] said that insulin level may decrease after death.…”

Section: Human Insulin Synthetic Insulin Analogues C-peptide and Prmentioning

confidence: 98%

“…The activity of IDE is decreased at 4°C or -20°C and insulin in blood and plasma samples is relatively stable (for at least 5 days [111] at 4°C). Serum collected at autopsy must be separated from cellular elements immediately and stored at −20°C [25,66,[112][113][114][115] at which insulin is stable for several months, C-peptide for at least 40 days. However, a stability at 4°C for C-peptide is not given [63].…”

Section: Analytical Interferences and Sample Storage For The Peptidesmentioning

confidence: 99%

See 2 more Smart Citations

Disorders of glucose metabolism: post mortem analyses in forensic cases–part II

2010

View full text Add to dashboard Cite

In continuation to part I, a literature review is presented concerning biochemical problems of forensic post mortem cases of unclear hyperglycaemia or hypoglycaemia. Clinical parameters for this purpose were recently reviewed. Particular attention was paid to the detection of diabetic ketoacidosis, of hyperosmolar coma, insulinoma, insulin-induced or oral diabetic-induced hypoglycaemia. The second part of the review discusses the analytes ketone bodies, synthetic insulins, human insulin, C-peptide, proinsulin and insulin antibodies. Special interest is given to post mortem matrices for those analytes to reference concentrations, stability data, analytic interferences and analytical procedures which should be used in toxicological laboratories willing to detect diabetic metabolism disorders after death.

show abstract

Section: Analytical Interferences and Sample Storage For The Peptidesmentioning

confidence: 98%

Section: Human Insulin Synthetic Insulin Analogues C-peptide and Prmentioning

confidence: 98%

Section: Analytical Interferences and Sample Storage For The Peptidesmentioning

confidence: 99%

See 1 more Smart Citation

Disorders of glucose metabolism: post mortem analyses in forensic cases–part II

2010

View full text Add to dashboard Cite

show abstract

“…Recently. significant progress has been made in the study of the ATP-binding site by using [71.____ ~~ vanadate, which is considered a good structural analogue of phosphate [14]. The S1 95-kDa heavy chain is specifically cleaved by near-ultraviolet irradiation in the presence of vanadate at sites 23-kDa and 74-kDa from the N-terminus, and regions in the vicinity of these cleavage sites were assumed to be the phosphate-binding sites of S1 [15, 161.…”

mentioning

confidence: 99%

“…____ ~~ vanadate, which is considered a good structural analogue of phosphate [14]. The S1 95-kDa heavy chain is specifically cleaved by near-ultraviolet irradiation in the presence of vanadate at sites 23-kDa and 74-kDa from the N-terminus, and regions in the vicinity of these cleavage sites were assumed to be the phosphate-binding sites of S1 [15, 161. The cleavage site at 23 kDa from the N-terminus was localized at Serl80 [17], supporting the conclusions of the homology analysis, viz.…”

mentioning

confidence: 99%

Effects of ions on vanadate‐induced photocleavage of myosin subfragment 1

Mühlrád

Peyser

Ringel³

1991

European Journal of Biochemistry

View full text Add to dashboard Cite

Myosin subfragment 1 (Sl) is cleaved by near-ultraviolet irradiation in the presence of vanadate at three sites located at 23, 31 and 74 kDa from the N-terminus. Since vanadate is considered to be a good structural analogue of phosphate. it is assumed that the cleavage sites participate in forming the phosphate-binding site(s) of S1. In this work. the effect of various ions on the vanadate-induced photocleavage of S1 was studied. Monovalent anions were found to inhibit photocleavage in the 50-200 mM range. The inhibition is more expressed at a site 74 kDa from the N-terminus than at the 23-kDa and 31-kDa sites. The inhibitory effect of the monovalent anions increases in the order acetate = F-< CI-< Br-< I-= S C N -. The order of the inhibitiory effect is identical to the protein-structure-damaging effect of monovalent anions in the von Hippel series [von Hipel, P. (1 964) Scimce 145,577 -5811. 'Therefore, it is assumed that decreased photocleavage is due to local perturbations of structure, especially at the 74-kDa site, in addition to increased ionic strength. Divalent anions, sulfate and thiosulfate, strongly inhibit photocleavage at 2 mM. The inhibition is very pronounced at the 23-kDa and 31-kDa sites, while the 74-kDa site is hardly affected. Since photocleavage at the 23-kDa and 31-kDa sites is regulated jointly and independently from cleavage at the 74-kDa site, it is assumed that S1 has two distinct phosphatebinding sites: the regions of the 23-kDa and 31-kDa cleavage sites, which are proximal to each other in the spatial structure. participate in forming the first phosphate-binding site, while the 74-kDa site is part of the second binding site. Sulfate was also found to inhibit the trapping of vanadate and to facilitate its release from the S1-MgADP-V, (Vi, inorganic vanadate) complex. Photocleavage of S1 takes place at all three sites, both in the presence or absence of divalent cations, indicating that these, including Mg2', are not essential for cleavage.The interaction of myosin with actin and ATP generates the driving force of muscle contraction. 'The distinct ATPbinding and actin-binding sites of myosin reside on the globular head segment of the molecule. Due to the significant functional role of myosin-ATP and myosin-actin interactions, it is important to characterize the respective binding sites on myosin subfragment 1 (Sl). In spite of considerable efforts [l], the ATP-binding and actin-binding sites remain only partially characterized. According to studies which include limited tryptic digestion [2, 31, covalent cross-linking [4, 51 and the use of a specific antipeptide [6], at least part of the actinbinding site resides on the stretch at residues 632-643 of S1, at thejunction of the 50-kDa and 20-kDa tryptic S1 fragments Attempts to asign the ATP-binding site have been made using photoaffinity analogues of ATP [8 -111 and by analysis based on homology with other ATP-binding proteins [12. 131. On the basis of homology, a characteristic GXXXXGK sequence, corresponding to the stretch at residue...

show abstract

Radioimmunoassay of Drugs in Body Fluids in a Forensic Context

Smith

1988

Forensic Science Progress

View full text Add to dashboard Cite

Insulin in post-mortem blood

Cited by 23 publications

References 4 publications

Disorders of glucose metabolism: post mortem analyses in forensic cases–part II

Disorders of glucose metabolism: post mortem analyses in forensic cases–part II

Effects of ions on vanadate‐induced photocleavage of myosin subfragment 1

Radioimmunoassay of Drugs in Body Fluids in a Forensic Context

Contact Info

Product

Resources

About