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Biomedical subjects

K Kithier

Publications and source records attributed to K Kithier.

At least 37 records · Page 2Linked to original sources

Multiple forms of bovine kidney alkaline phosphatase.

Partial purification of bovine kidney alkaline phosphatase produced two fractions (F1, F2). Double immunodiffusion experiments using antiserum against the pooled kidney fractions showed a complete fusion of the precipitin line of bovine kidney F2 with those of bovine kidney F1, liver, bone, and placental alkaline phosphatases. No reaction was observed between the antiserum and alkaline phosphatase from either bovine intestine or human kidney. Crossed immunoelectrophoresis of fraction F2 produced two peaks that crossed each other and stained for enzyme activity. This finding is discussed in light of recent reports of multiple antigenic forms of alkaline phosphatase form human and rabbit kidney.

Alkaline Phosphatase↗

Glomerular permeability to endogenous proteins in the rat: effects of acute hypertension.

The distribution of endogenous albumin and immunoglobulin G (IgG) has been studied by the immunoperoxidase technique in the superficial glomeruli of both normotensive and hypertensive (acute angiotensin II-induced) Munich-Wistar rats. Endogenous IgG has also been detected in rats immunized with horseradish peroxidase. Labeled antibodies have been applied to sections on a conventional manner as well as by an electrophoretic technique. The immunization of animals with horseradish peroxidase, as well as application of the electrophoretic technique, both result in a greater yield of labeled glomeruli. Albumin is present within the capillary lumina of control animals, penetrates the capillary walls, and extends into the urinary space. Endogenous IgG is mainly confined to lumina of glomerular capillaries, with only small amounts visible in the laminae rarae of the basement membrane. After acute hypertension induced by angiotensin II, there is increased staining of albumin and IgG in the basement membrane and of albumin in the urinary space. There is also penetration of IgG into Bowman's space. Both macromolecules are found in dilated mesangial channels. These modifications of glomerular permselectivity in hypertension are not accompanied by discernible ultrastructural changes in the peripheral capillary wall. It is suggested that the transcapillary passage of albumin and IgG is dependent upon hemodynamic factors and/or subtle changes in the filtering membrane.

Animals↗

The value of serial carcinoembryonic antigen (CEA) in predicting response rate and survival of patients with gastrointestinal cancer treated with chemotherapy.

Elevated serum levels of carcinoembryonic antigen (CEA) were found in 70% of 141 patients with advanced gastrointestinal (GI) cancers. Serial CEA measurements were performed on 70 patients before and during chemotherapy. The majority were treated with 5-FU and Methyl-CCNU (33 patients), 5-FU (19 patients), or 5-FU and mitomycin-C (8 patients). In 49 patients with colorectal carcinoma who had elevated serum CEA prior to chemotherapy, 18 had objective partial tumor remission, 16/18 (89%) showed definite decrease in CEA level, one had no change, and one had an increase CEA titer. Thirty-one patients had either stable disease (10 patients) or increasing disease (21 patients) while on chemotherapy. Of these patients four showed decrease in CEA, eight had no change, and 19 had increase in CEA levels as compared to pretreatment value. The survival of patients with a decrease in CEA during chemotherapy was statistically significant (p = .03) as compared to survival of those with no change or increasing CEA levels. In 21 patients with other GI cancers, the correlation between the clinical response and change in CEA level observed was not as definite as in patients with colorectal carcinoma.

Adenocarcinoma↗

IgD myeloma protein with "unreactive" light chain determinants.

Serum from a patient with multiple myeloma showed a monoclonal protein, classified by immunoelectrophoresis as IgD. Immunofixation electrophoresis and immunoelectrophoresis failed to demonstrate a precipitation reaction between the paraprotein and antisera to immunoglobulin light chains. The light chains of the monoclonal protein, immunologically inaccessible in the intact molecule, reacted with anti-lambda chain antisera only after reduction and alkylation of the paraprotein. Moreover, interpretation of the immunoelectrophoretic patterns was hampered by the presence in patient's serum of free lambda chains having about the same mobility as that of the paraprotein.

Aged↗

Binding of 17beta-estradiol by variants of alpha-fetoprotein in rat amniotic fluid.

Two variants of alpha-fetoprotein in rat amniotic fluid were separated by their different affinity for concanavalin A-Sepharose, which selectively binds alpha-D-manno-pyranosides and alpha-D-glucopyranosides. Both forms had the same mobility upon polyacrylamide gel electrophoresis. The binding of 17beta-estradiol per mg of alpha-fetoprotein, determined both immunologically and electrophoretically, was the same for both variants. These results indicate that a specific carbohydrate portion of the molecule is not necessary for steroid binding.

Amniotic Fluid↗

Beta2-microglobulin in human colostrum and milk: effect of breast feeding and physico-chemical characterization.

A statistically significant increase in beta2-microglobulin concentration in babies' sera after birth was accompanied by a decrease in beta2-microglobulin concentration in sera of nursing and non-nursing mothers; the amount by which babies' sera concentrations increased was not correlated with the decrease in serum or milk concentrations in their mothers. These results suggest that breast feeding does not affect the concentration of beta2-microglobulin in babies' sera. Furthermore, there was no relationship between serum beta2-microglobulin concentration of mothers and their babies at either point of observation. In all instances, however, the beta2-microglobulin concentration was significantly higher in infants' sera than in mothers' sera.

Breast Feeding↗