[Local anesthetic effect of phenol derivatives. 2. Eugenol and guaiacol].
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Anesthetics, Local↗
Biomedical subjects
M Ehara
Publications and source records attributed to M Ehara.
Serum lipase response to cerulein secretin stimulation test in patients with pancreas-associated diseases as measured by sensitive colorimetric assay (a BALB-DTNB method).
We have compared responsiveness of serum lipase and amylase activity to the pancreatic exocrine stimulation with cerulein and secretin (CS test) in normal subjects and patients with pancreas-related and other diseases. The lipase and amylase activities were measured by a sensitive colorimetric method, the BALB-DTNB method and the Caraway method, respectively. The percentage of positive lipase and amylase response cases was as follows: confirmed chronic pancreatitis (N = 22), 27 and 14%; suspected chronic pancreatitis (N = 37), 46 and 32%; pancreatic cancer (N = 16), 44 and 25%; biliary tract diseases (N = 11), 14 and 14%; miscellaneous (N = 11), 0 and 18%; normal subjects (N = 13), and partial pancreatectomy (N = 5), 0 and 0%, respectively. The serum lipase response cannot be regarded as specific for pancreatic diseases because the lipase response cases were found in biliary tract diseases as well. However, in view of frequent, fast, and intense responsiveness to the CS test, the serum lipase activity measured by the BALB-DTNB method may be more useful than the serum amylase as an auxiliary diagnostic aid for suspected pancreatitis which might develop into confirmed chronic pancreatitis or cancer of the head or body of the pancreas.
Adolescent↗
[Local anesthetic effects of phenol].
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Anesthetics, Local↗
Effect of albumin on amylase assay using blue starch polymer.
The nature of the stimulation by albumin of amylase activity determined by use of blue starch polymer was studied. The binding of albumin to the starch polymer was responsible for the stimulation of amylase activity, since the stimulation was observed with the albumin-bound blue starch polymer as substrate irrespective of the presence or absence of free albumin in the reaction mixture. When the albumin-bound blue starch polymer was hydrolysed by amylase, the blue oligosaccharide fragments were released with the albumin attached. These oligosaccharide fragments were about 1.3 times larger in average molecular size than the fragments released in the absence of albumin, suggesting that the apparent stimulation of amylase by albumin, (about 1.3 times) is due to the liberation of the larger oligosaccharide fragments.
Amylases↗
Coexistence of bilateral pheochromocytoma and pancreatic islet cell tumor: report of a case and review of the literature.
A 14-year-old Japanese male with a previously undescribed combination of bilateral pheochromocytoma and an islet cell tumor of the pancreas is presented. The combination of endocrine neoplasms in this patient overlaps multiple endocrine neoplasia (MEN) Type 1 and Type 2. A total of 14 reported cases of MEN overlapping Type 1 and Type 2 is reviewed. Of the 14, 7 patients with acromegaly developed a paraganglioma(s), 2 patients with Sipple syndrome had a pituitary adenoma, and in the other 5 patients, an intestinal carcinoid or a pancreatic islet-cell tumor occurred in association with either a thyroid medullary carcinoma or a paraganglioma(s). We believe that the occurrence of MEN overlapping Type 1 and Type 2 is more than a fortuitous association, and can be explained on the basis of the neuroectodermal origin.
Adenoma, Islet Cell↗
A study on the nature of macroamylase complex. Dissociation of macroamylase by substrates.
Characteristics of a macroamylase that was considered not to be formed by the binding of normal amylase to immunoglobulins were studied. The macroamylase was reversibly dissociated into apparently normal amylase by treating the macroamylasemic serum with guanidine hydrochloride. Concanavalin A precipitated a large portion of the macroamylase. When the macroamylase was purified by affinity chromatography using an insoluble starch polymer at neutral pH, a considerable dissociation of the enzyme into apparently normal amylase was observed with the purified preparation. Such dissociation of the macroamylase was demonstrated by briefly incubating the patient's serum with a low-molecular weight starch, a substrate of the enzyme. This dissociated enzyme showed upon electrophoresis essentially the same isozymic pattern as that of normal serum amylase. When the patient's serum was incubated with the low molecular weight starch for a prolonged period to hydrolyze the starch completely and was dialyzed, reconstitution of macroamylase resulted. The amylase-binding substance(s) that is supposed to be involved in the formation of macroamylase was found to release when the enzyme was adsorbed on the insoluble starch polymer at 0 degrees C. The present results strongly suggest that the amylase-binding substance(s), probably polysaccharide(s) or glycoprotein(s), binds to the substrate-binding site of normal amylase to form a macroamylase complex.
Adsorption↗