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K D Gerbitz

Publications and source records attributed to K D Gerbitz.

79 records · Page 5Linked to original sources

Free insulin, bound insulin, C-peptide and the metabolic control in juvenile onset diabetics: comparison of C-peptide secretors and non-secretors during 24 hours conventional insulin therapy.

In two groups of juvenile onset diabetics similar in age, weight, diet and daily insulin dosage (eight without C-peptide, group I; eight with C-peptide, group II) the serum levels of free and antibody bound insulin, C-peptide, glucose, lactate, alanine and FFA were determined over 24 h. In addition the affinity and binding capacity of the insulin antibodies were determined in vitro. No correlation was found between free or bound insulin and glucose. This holds true for the individual profiles as well as for the averaged profiles of the two groups. Free insulin and lactate or alanine were positively correlated in the C-peptide secreting group. C-peptide secretion followed the flucturations of the glucose level during 24 h in each individual patient. As a group, C-peptide secretors were better controlled than non-secretors with respect to mean blood glucose, M-value and the lability index and showed higher free insulin levels despite a similar daily insulin dosage. The possible reasons for this fact are discussed. No correlation was found between the affinity characteristics of the insulin antibodies and the degree of metabolic control or the daily insulin dosage.

Adolescent↗

Human alkaline phosphatases. I. Purification and some structural properties of the enzyme from human liver.

Alkaline phosphatase (EC 3.1.3.1) from human liver was purified to homogeneity. It is a glycoprotein of about 136000 molecular weight. Analysis of the subunit structure by sedimentation equilibrium in 6M urea and by dodecylsulfate polyacrylamide gel electrophoresis of the denatured enzyme indicated molecular weights of about 35000 and 32000, respectively. Thus, the human liver alkaline phosphatase seems to be a tetramer composed of identical or very similar subunits. The purified enzyme has a specific activity of 1360 mumol/(min x mg prot.), corresponding to a molecular activity of 3170s-1. The enzyme retains full activity in 1% sodium dodecylsulfate for several hours. The isoelectric point of the native enzyme is 4.2. After treatment with neuraminidase the isoelectric point increases to 6.5.

Alkaline Phosphatase↗

Human alkaline phosphatases. II. Metalloenzyme properties of the enzyme from human liver.

Human liver alkaline phosphatase is a metalloenzyme requiring Zn2 and Mg2 for full activity. Zn2 cannot be replaced by manganese, cobalt or calcium, whereas Mg2 can be replaced by manganese or calcium. The binding constants of the enzyme for different divalent cations were determined by the use of complexing agents. The enzyme is inhibited by a number of reducing and complexing agents such as 2-mercaptoethanol, cyanide, nitrilotriacetic acid and EDTA. From studies using these inhibitors it is suggested that there are different mechanisms of inhibition. Reversible inhibition occurs if the free Zn2 concentration is not significantly lower than 10(-12)M. Inhibition is irreversible at lower Zn2 concentrations. Evidence is given, that the human liver alkaline phosphatase possesses different zinc binding sites, which are responsible for the catalytic function and for the integrity of the enzyme structure.

Alkaline Phosphatase↗

Clinical utility of nonenzymatically glycosylated blood proteins as an index of glucose control.

This study compares the utility of nonenzymatically glycosylated serum proteins (lys-GSP) to glycosylated hemoglobins (HbA1a-c) as control indices of glucose homeostasis in patients with IDDM. The diagnostic value of lys-GSP was also examined in patients with non-insulin-dependent diabetes mellitus, in subjects with impaired glucose tolerance, and in two patients with insulinoma. The intraindividual fluctuation of lys-GSP in normoglycemic subjects is very small, resulting in an interindividual range of 3.0 +/- 0.3 lysine-bound glucose/mg protein (means +/- SD, N = 52). HbA1a-c with a normal range of 6.4 +/- 0.9% (N = 52) shows greater variability. In IDDM there is no overlap of lys-GSP levels between the normal and the diabetic range at the 95% confidence level. In patients treated with an open-loop insulin delivery system failure of normalization of the glucose balance was clearly discernible by an elevation of GSP. In contrast, in about 40% of the patients with incomplete glycemic control the HbA1a-c levels fell within the normal range. The utility of lys-GSP for diagnosis of diabetes is compared with the results of 60 oral glucose tolerance tests. Two patients suffering from insulinoma displayed decreased lys-GSP values. From these results it appears that determination of lys-GSP represents a more sensitive parameter for long-term control than HbA1a-c and is suitable for monitoring even small fluctuations of blood glucose.

Adolescent↗