Tumor Amylase Research Articles

腫よう産生アミラーゼの電気泳動的分析

Amylase-producing tumors are mainly lung cancer, ovarian cancer and myeloma. The type of isoamylase produced by the tumors is exclusively of the salivary type (s-). Therefore, hyper s-amylasemia is a valuable aid in the diagnosis of amylase-producing tumors, however, occurs in a large variety of conditions. This paper reports the clinical laboratory findings indicating of presence of tumor amylase. One hundred and eighty sera from 85 patients with primary lung cancer and 185 sera from patients with hyper s-amylasemia, but not suffering from lung cancer, ovarian cancer or myeloma, were studied for the presence of tumor amylase by amylase activity measurement and isoamylase electrophoresis. A persistently increased value for amylase in serum and/or a S3 isoform/S2 isoform activity ratio of greater than 33% were a useful indicator of the presence of tumor amylase. An incidence of amylase-producing tumor of 7% among the 85 cases of primary lung cancer was found.

Amylase from human serous ovarian tumors: purification and characterization.

Human serous-type ovarian tumors contain an acidic isoenzyme of amylase. Previous attempts at purification of tumor amylases have yielded preparations contaminated with other proteins. The purification scheme presented here incorporates an affinity-chromatography procedure, with use of cycloheptaamylose linked to epoxy-activated Sepharose, that is specific for alpha-amylase (EC 3.2.1.1). Purified amylase isoenzyme from a human serous ovarian tumor was characterized and compared with the purified salivary and pancreatic isoenzymes. All three were similar in amino acid composition, pH optimum, substrate specificity, calcium requirement, heat inactivation, and Km for maltotetraose substrate. The ovarian tumor amylase was similar to the salivary and distinct from the pancreatic enzyme by apparent molecular mass and doublet formation on sodium dodecyl sulfate--polyacrylamide electrophoresis, specific activity of pure enzyme, and sensitivity to specific alpha-amylase inhibitors. All three isoenzymes differed in net electrical charge as evidenced by diethylaminoethyl-Sephadex ion-exchange chromatography and isoelectric focusing. The tumor amylase is clearly distinct from the pancreatic and differs from the salivary enzyme in net electrical charge. Evidence is presented that this charge difference may reflect, at least in part, deamidation of an amylase that is similar to or identical with salivary amylase.

Improved DEAE-Sephadex column chromatography in measuring amylase in serous ovarian neoplasms, and results for 13 cases.

We describe a column-chromatographic method for measuring amylase activity in cyst fluids of serous ovarian tumors. Using this technique, we confirm and extend the previous report of an "acidic" amylase in serous ovarian tumor cyst fluids. This form of the enzyme was eluted from DEAE-Sephadex mini-columns with a high-salt buffer. It accounted for 45 to 100% of the amylase in 13 cyst fluids. This "high-salt" amylase was also present in the tumor tissues. The acidic nature of the amylase does not appear to be due to sialic acid residues, because the chromatographic behavior of the amylase is unaffected by treatment with neuraminidase. We conclude that the "acidic" amylase reported previously in two serous ovarian tumors is a constant feature of these tumors and that it is distinct from the sialylated tumor amylase described by others.

Properties of the amylase produced in carcinoma of the lung

The properties of the amylase produced by carcinoma of the lung were studied. The abnormal amylase recognized in the serum of a patient with carcinoma of the lung had a mobility with beta-position and showed reduced migration to the cathodic side after neuraminidase digestion. This abnormal amylase had a close affinity for Concanavalin A and this affinity was not retarded by the neuraminidase digestion. However, the purified, tumor-extracted, amylase from the same patient had the same electrophoretic migration as normal human salivary amylase and was not affected by neuraminidase treatment. The abnormal affinity for Concanavalin A was not observed in this purified tumor-extracted amylase. It is suggested that some transglycosidation steps are needed for the appearance of the abnormal amylase in the patient's serum, and that the terminal sialic acid is independent of the affinity for Concanavalin A. The dissociation constants of the tumor amylase for several substrates were smaller than those of normal pancreatic or salivary amylases. Moreover, maltotriose had no affinity for the tumor-extracted amylase and it was not digested to maltose and glucose by the purified tumor extracted amylase. These differences in the kinetic properties and in the mode of digestion were of interest in the study of tumor-produced amylases.

Bibliographical Index

Bibliographical IndexPublished Online:29 May 2014https://doi.org/10.1259/0007-1285-7-77-315SectionsPDF/EPUB ToolsAdd to favoritesDownload CitationsTrack Citations ShareShare onFacebookTwitterLinked InEmail AboutAbstractMarch 1934. Dilatations of the cavity of the septum pellucidum and cavum vergæ (W. P. Van Wagenen and Robert B. Aird). Effect of radium on the spinal cord (W. T. Peyton). Union of pathological fractures following metastatic hypernephroma (E. L. Rypins). An accidental autogenous transplantation of a mammary carcinoma to the thigh during a skin-graft: case report (J. W. Spies, F. E. Adair, and M. C. Jobe). Nematode and carcinoma in human kidney pelvis (Alfred Plaut). Tumor amylase: general properties and estimation of activity (F. H. Scharles and W. T. Salter). Tumor amylase: the effect of various hormones and chemical agents (F. H. Scharles, Phœbe D. Robb, and W. T. Salter). Previous article Next article FiguresReferencesRelatedDetails Volume 7, Issue 77May 1934Pages: 257-320 © The British Institute of Radiology History Published onlineMay 29,2014 Metrics Download PDF