Assessment of electrophoretic mobilities of some human isoamylases

A, Vacíková

doi:10.1016/s0021-9673(00)92904-2

Cited by 12 publications

(4 citation statements)

References 5 publications

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“…4] and a variety of other diseases. The presence of high levels of amylase activity in the contents of cysts derived from the mullcrian or mesonephric duct [1,7,8] lias led to the conclusion that there is local produc tion of amylase in the epithelium of the human genital tract. Tissue homogenates of human fallopian tube and cervical mucosa, but not endometrium, were found to contain specific genital isoamylases [1], and several authors [25,26] have demonstrated increased amylase levels in human fallopian tube fluid.…”

Section: Discussionmentioning

confidence: 99%

An Amylase-Producing Serous Cystadenocarcinoma of the Ovary

Hodes

Sisk²,

Karn³

et al. 1985

Oncology

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A patient with an amylase-producing serous cystadenocarcinoma of the ovary had elevated serum and urine amylase levels and high levels of amylase in pleural and ascitic fluids. Serum and urine amylase levels reflected both surgical removal of tumor mass and response to chemotherapy. Tumor homogenates had pronounced amylase activity. Salivary type amylase isozyme patterns were found in electrophoresis of samples from all sources. Ascites tumor cells were successfully cultured and salivary type amylase was found in the culture media throughout 5 passages. The tumor was classified by light microscopy as poorly differentiated serous cystadenocarcinoma. Ultrastructural studies on the tumor were consistent with that diagnosis. Amylase was detected in the cells of the tumor examined by the immunoperoxidase technique.

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Section: Discussionmentioning

confidence: 99%

An Amylase-Producing Serous Cystadenocarcinoma of the Ovary

Hodes

Sisk²,

Karn³

et al. 1985

Oncology

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“…The supernatant was dialyzed against distilled water for 24 hr using a multiple sample dialyzer. 1 The dialysate was then frozen and lyophilized. To prepare stock solutions, 50 mg of the lyophilized product was dissolved in 100 ml of sodium phosphate buffer, pH 6.9, to give a 0.05% solution of inhibitor.…”

Section: Methodsmentioning

confidence: 99%

Clinical Science Population Distribution of Human Salivary Amylases: Differential Inhibition by Wheat Protein

Gertzman¹,

Rivas²,

Strumeyer

1980

J Dent Res

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Based upon response to an inhibitor from wheat gliadin, 80 random samples of human salivary amylase were separated into three phenotypic groups. Each phenotype occurred with a high frequency rendering this a polymorphinc locus. The susceptibility to the inhibitor may be a useful marker for studies of tendency to caries and periodontal disease as well as for studies of genetic variation and linkage.

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“…The pancreatic-like isoenzyme of serum could be resolved into two bands (44), and it was subsequently reported that the salivary-like isoenzyme could likewise be resolved into two bands (138). Isolation o f pancreatic-like and salivary-like amylases from human serum and urine was also achieved by means o f gel filtration and ion-exchange chromato graphy (51), and clinical studies established the pancreas as the probable source o f pancreatic-type amylase in human serum; however, other human tissues con tain amylases with chromatographic properties similar to those o f pancreas and salivary glands.…”

Section: Isoamylasesmentioning

confidence: 99%

Amylase, Isoamylase and Macroamylase

Goldberg¹,

Spooner²

1975

Digestion

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Hyperamylasaemia has long been regarded as pathognomonic of acute pancreatitis. However, recent work has revealed a number of conditions where a gross elevation may be an incidental finding, notably diabetic ketoacidosis. The recent discovery of ‘macroamylase’, a high molecular weight amylase-protein complex capable of producing hyperamylasaemia with low urine amylase, has further complicated diagnosis and has led to the introduction of the ratio of amylase clearance to creatinine clearance as a diagnostic aid. Serum amylase may be resolved, by most electrophoretic media, into bands which correspond to those obtained when pancreatic homogenates or saliva are electrophoresed. The initial promise of this technique has not been realised at the routine diagnostic level. Duodenal juice amylase has been the classical enzyme used in assessing exocrine pancreatic function and although it is still of value it is being amplified by other enzyme tests.

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Assessment of electrophoretic mobilities of some human isoamylases

Cited by 12 publications

References 5 publications

An Amylase-Producing Serous Cystadenocarcinoma of the Ovary

An Amylase-Producing Serous Cystadenocarcinoma of the Ovary

Clinical Science Population Distribution of Human Salivary Amylases: Differential Inhibition by Wheat Protein

Amylase, Isoamylase and Macroamylase

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