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Biomedical subjects

S Matzku

Publications and source records attributed to S Matzku.

At least 91 records · Page 5Linked to original sources
PubMed1978

Radioimmunological quantitation of human group-II pepsinogens.

A solid-phase sandwich radioimmunoassay was developed to quantitate human group-II pepsinogens in plasma. The test detected pepsinogen II in a concentration range of 0.25--64.0 ng/ml using sample volumes of 125 microliter. Purified group I pepsinogens showed no response up to concentrations of 100 microgram/ml. In apparently healthy donors, we observed mean plasma concentrations of 20.3 ng/ml (males) and of 15.5 ng/ml (females).

Antibodies↗
PubMed1978

[Leukocyte migration test and determination of carcinoembryonic antigens in the postoperative follow-up care of colon and rectum carcinoma].

Preoperative and serial postoperative CEA determinations have become widely accepted tools to aid the early detection of recurrent colorectal cancer. The panel modification of the direct leukocyte migration test (LMT) has proved to be an excellent monitor in these tumor patients. In this study LMT and CEA-RIA were compared. Peripheral blood leukocytes were pulsed with a high dose (2.5 and 0.5 mg/ml) of 3 m KCl extracts of five different colorectal tumors as well as with one 3m KCL extract of normal colonic mucosa. Patients showing a pathologic migration index (less than 0.80 and greater than 1.17) of 3 or more out of five tumor extracts were considered to be "positives." With this test mode 51 of 59 (86%) patients with resectable tumors were reactive, while only 24 of 69 (41%) yielded elevated CEA values. Both LMT and CEA-RIA were positive in 12 of the 13 patients with nonresectable tumors. After curative surgery most patients' leukocyte migration and CEA values were in tne normal range. Of the nine patients with localized tumor recurrence, eight were LMT reactive and five showed elevated CEA values. Of five patients with distant metastases, four demonstrated a positive reaction in the LMT and five a rise in CEA levels. The combination of the LMT with the CEA-RIA promises to improve the detection of recurrent colorectal cancer before the appearance of clinical evidence of recurrence.

Carcinoembryonic Antigen↗
PubMed1977

Leukocyte migration studies in gastric cancer detection: an approach toward improved specificity and sensitivity.

Peripheral blood leukocytes from patients with gastric cancer and various other malignant and nonmalignant diseases and peripheral blood leukocytes from apparently healthy volunteers were tested in the leukocyte migration inhibition test with the use of 4-5 different 3 M KCl extracts of gastric cancer tissue. An operational criterion for defining sensitization of patients' leukocytes was developed; i.e., evidence in an individual sample of leukocytes of either decreased or increased migration areas (migration index less than or equal to 0.79 and larger than or equal to 1.20, respectively) with 3 or more antigen extracts. With this as an indicator of sensitization, it was found that 91% of patients with gastric cancer (39/43), comparto 5% (5/94) and 3% (1/32) of patients with nonmalignant, nongastric diseases and normal controls, respectively, were reactive. Patients with various nongastric cancers were sensitized in 36% (49/135) of cases. Gastritis and gastric, as well as duodenal, ulcer did not influence the reactivity of patients' leukocytes, but considerable sensitization was found in patients with atrophic gastritis or intestinalization. When classified in the usual manner, i.e., by considering the reaction with individual tumor extracts, the specificity and the sensitivity of the test was markedly diminished: More false negative determinations were found in the group of gastric cancer patients, and the percentage of false positives in the group of nonmalignant diseases increased. The results gave evidence of tumor-associated antigens in gastric cancer patients, against which the host elicited a cellular immune response. The high incidence of positive reactivity of leukocytes from patients with gastric cancer, together with the considerable cross-reactivity of leukocytes from patients with nongastric cancer, pointed to the expression of antigens with organ-related and widespread specificities.

Adult↗
PubMed1977

A modified leucocyte migration assay as indicator of malignant and non-malignant gastric mucosal alteration.

When gastric cancer patients' leucocytes were exposed to a panel of tumour extracts, leucocyte migration reactivity was "positive" before operation (90% of cases), it declined after surgery and it reappeared in patients with local recurrence or metastases. In patients with non-malignant gastric diseases, "positive" reactivity against tumour extracts was associated almost exclusively with atrophic gastritis with and without intestinal metaplasia (24/43 cases). "Positive" patients also showed a pathological migration index with an extract of normal gastric mucosa.

Adult↗
PubMed1977

[Improvement of specificity and reactivity of the leukocyte migration test for the diagnosis and follow-up care in stomach cancer].

The leukocyte migration assay proved to be a very sensitive tool in gastric cancer diagnosis. When patients' leukocytes were exposed to a panel of 3m KCl extracts, positive reactivity was found at a rate of 92%. All patients with non-malignant gastric diseases exhibiting "positive" reactivity with gastric tumor extracts also showed a pathological migration index with a 3m KCl extract of normal gastric mucosa, while only in 16% of patients with gastric cancer leukocyte migration was influenced by this extract. Using gastric tumor extracts patients with colorectal cancer showed a cross-reactivity in 67% and patients with carcinoma of the pancreas and oesophagus in 42% of the tests. Three months after curative surgery most patients' leukocyte migration was found to be in the normal range. Positive reactivity reappeared in patients with local recurrence or metastases.

Cell Migration Inhibition↗
PubMed1976

Purification of human gastric proteases by immunoadsorbents: pepsinogen II-group.

The pepsinogen II group was prepared from gastric mucosal extract by a two-step procedure consisting of immunoadsorption to an anti-pepsinogen II column, followed by ion exchange chromatography on DEAE-Sephadex A-50. The final product was pure according to biochemical and immunochemical criteria. As determined by quantitative immunodiffusion, the enrichment factor of pepsinogen II was 34. A recovery of 55% was calculated. The effectiveness of this procedure was due to the use of purified anti-pepsinogen II antibodies for immunoadsorption. This was achieved by immunoadsorption to Sepharose bound crude pepsinogen and a further passage over an unrelated immunoadsorbent (human serum coupled to Sepharose). The immunoadsorbent prepared using purified anti-pepsinogen antibodies showed low non-biospecific binding of gastric extract proteins. Complete separation of pepsinogen II from pepsinogen I was observed in one single passage. Purified pepsinogen II showed two protein bands in polyacrylamide gel electrophoresis and four bands of proteolytic activity in agarose enzyme electrophoresis. In both methods, as well as in two-dimensional immunoelectrophoresis, components with the same electrophoretic mobility were detected in pure preparations of group and II pepsinogens. Consequently, only in pure preparations was it possible to define the exact number of bands belonging to each of the two groups and to assess the immunological specificity of every band. Upon hydroxyapatite chromatography purified pepsinogen II was further resolved into two fractions.

Blood Proteins↗
PubMed1976

Purification of human gastric proteases by immunoadsorbents. Pepsinogen I group.

Human pepsinogen I group was purified by immunoadsorption techniques. Gastric mucosal extracts containing the pepsinogen I group and the pepsinogen II group and concentrated urine containing only pepsinogen I group were separated by DEAE-ion-exchange chromatography to remove the bulk of human serum protein. Fractions displaying proteolytic activity were further purified by adsorption on an anti-pepsinogen I group Sepharose immunoadsorbent column. After desorption, gastric pepsinogen I group was separated from pepsinogen II group. Trace amounts of contaminating protein were removed from preparations from gastric mucosal extracts and urine by passage over an anti-human serum immunoadsorbent column. The purity of pepsinogen I group from both sources was assessed by electrophoretic and immunological criteria. The isolated pepsinogen I group from gastric mucosal extracts and urine were by biochemical and immunochemical criteria identical with each other and with the pepsinogen I group in the unfractionated starting materials. By agarose enzyme electrophoresis four bands were detected and it was determined that the proteases of the pepsinogen I group express the same individual antigenic determinant.

Adult↗
PubMed1976

Antigen and antibody purification by immunoadsorption: elimination of non-biospecifically bound proteins.

Immunoadsorption is a simple and effective method for purifying antigens and antibodies. The major interfering effect is non-biospecific binding, especially when crude preparations of antibodies or antigens are coupled to the matrix. In this paper various possibilities for eliminating these effects are compared and analysed. It was found that for antigen (AFP) purification pre-elution with a pH 10.0 buffer of high ionic strength (1.0 M) is effective. A major problem in purifying antibodies in the non-biospecific binding of IgG. This can be eliminated by using a non-biospecific immunoadsorbent column, where specific antibodies are not, or only weakly bound and IgG with irrelevant specificity but exhibiting high non-biospecific interaction is retained. This has been applied to preparation of sheep anti-pepsinogen II group protease antibodies.

Absorption↗
PubMed1975

Quantitation of alpha1-acid glycoprotein in neutralized gastric juice by electroradioimmunoassay (ERIA).

Alpha1-Acid glycoprotein (AGP) was quantitated by an electroradioimmunoassay (ERIA) in in vivo neutralized gastric juice (nGJ) of 226 patients, including normals and patients with various gastic diseases. The accuracy of ERIA was tested by extraction and recovery experiments. A possible interference of nGJ constituents with the quantitation procedure was excluded. The mean AGP concentration in gastric juice of normals was 1.04 mu/ml (range 0.04-4.1 mu/ml). The concentration was significantly higher in the gastric cancer group (mean 31.6 mu/ml, p less than 0.01), in the group of chronic metaplastic gastritis (mean 5.7 mu/ml, p less than 0.01) and in the group of BII resections (mean 8.8 mu/ml, p less than 0.05). In 6 out of 12 nGJ samples with high AGP concentrations, a spur formation (Ouchterlony type III) was observed in double gel diffusion when compared to serum AGP. In 3 out of these 12 samples, the dilution curve in ERIA differed from the serum AGP dilution curve. These results indicate a difference in the antigenic properties of AGP in nGJ.

Adolescent↗