abstract— Acid production activity (APA) in plaque suspensions from glucose, boiled soluble starch and hydrogenated starch hydrolysate (Lycasin®) was studied in 11 subjects. Amylase (alpha‐1,4‐glucan 4‐glucanohydrolase, EC 3.2.1.1) activity was measured in plaque and whole saliva samples from the same persons. Lycasin was found to be hydrolyzed by salivary amylase under the formation of di‐ and oligosaccharides, however, with a lower rate than starch. A high correlation was found between APA from glucose and from soluble starch and between APA from soluble starch and plaque amylase activity. No correlation was found between amylase activity in saliva and APA from soluble starch or between amylase activity in saliva or plaque and APA from Lycasin. APA from Lycasin was about 62% and from soluble starch about 76% of the APA from glucose. 0–25% of the total number of cultivable microorganisms from the plaque produced extracellular starch‐degrading enzymes. No correlation was found between number of starch‐degrading microorganisms and APA from soluble starch or between these numbers and the plaque amylase activity. By electrophoreses only amylase fractions of human origin were found in whole saliva, plaque supernatants and plaque suspensions, indicating that the microbial amylase activity in the plaque is low compared with that of salivary origin.
SUMMARY The salivary and pancreatic isoamylases of serum were determined separately in 234 cases ofduodenoscopy and retrograde cholangiopancreatography. Successful pancreatic opacification was associated with pathologically high pancreatic serum amylase activities in 60% of the cases.Extensive opacification was associated with large increases of pancreatic serum isoamylases, the maximal rise recorded was 40 times the initial value. In spite of these striking chemical events only two patients developed clinical acute pancreatitis. There were some variations in pancreatic opacification and in the elevation of pancreatic serum amylase which seemed to depend upon the particular contrast material used. A rise of the salivary serum isoamylases caused pathologically high total serum amylase activities in 7% of the cases. High levels of pancreatic serum isoamylase activity before the time of examination did not result in any different pattern of hyperamylasaemia.
Ten days of total energy deprivation evoked the following endocrine changes in 12 healthy, normal‐weight males: early and marked reductions and increments in the blood levels of T3 and reverse T3, respectively, with rapid returns to pre‐starvation levels after refeeding; a slight and late decrease in the blood levels of T4; a minute reduction of the blood levels of TSH; a pronounced increase in the blood levels of growth hormone, but a return towards preexposure levels even before discontinuation of starving; a minor and gradual enhancement of the blood levels of cortisol, and an increase in nocturnal urinary adrenaline excretion. It is assumed that these changes reflect a complex regulatory mechanism, the purpose of which is to secure adequate energy supply to vital organs.
An electrophoretic technique for demonstrating amylase isoenzymes is described. After separation in an agarose gel containing a linear polyacrylamide polymer to reduce electroendosmotic flow, the amylase fractions are visualized by incubation with a commercially available dye-starch polymer (Phadebas Amylase Test). The technique detects amylase fractions with activities below 10 U/l. Some characteristic changes in such diseases as acute and chronic pancreatitis, cystic fibrosis of the pancreas, macroamylasemia and inherited variants as well as after maxillofacial surgery are mentioned.
The activities of serum lactate dehydrogenase (S-LDH) and S-LDH isoenzymes were determined in 252 patients with a history of testicular germ cell tumors (TGCT). Fifteen of 37 patients with TGCT lesions and seven of 215 without had raised levels of S-LDH (above 8.0 mukat/l (480 U/l)). Of the patients with TGCT lesions, four had only raised S-LDH-1 levels, one only raised S-LDH-2 (and normal S-LDH), two only raised S-LDH-3 (one with normal S-LDH), and 10 had five combinations of raised levels of S-LDH isoenzymes with a predominance of S-LDH-1. S-LDH and S-LDH-1 correlated significantly with the total tumor volume in the patients with TGCT lesions, especially pronounced in those with lesions from seminoma. Of 34 patients with TGCT metastases, 13 with raised S-LDH levels lived significantly shorter lengths of time than 21 with normal S-LDH. Similarly, 11 with raised S-LDH-1 (above 3.0 mukat/l (180 U/l) lived significantly shorter times than 23 with normal S-LDH-1. S-LDH is a valuable tumor marker in patients with TGCT, especially in those with seminoma. Routine determination of S-LDH isoenzymes in addition to S-LDH in patients with TGCT is not recommended. In patients with a history of TGCT and an unexplained elevation of S-LDH levels, a raised S-LDH-1 level indicates the presence of TGCT lesions.
Amylase activity and isoenzyme pattern were determined in human milk from various stages of lactation and were compared with that in duodenal juice. The activity is high in colostrum and somewhat lower in milk from day 15 to day 90 after delivery. In this period of lactation, human milk contains higher amounts of amylase than duodenal juice from infants aged 1 to 6 months. Low activity was found in milk from 90 days or more after delivery. The amylase is of the salivary type. A pH of 5.3 does not inactivate the amylase; there is considerable human milk amylase activity in duodenal juice after a meal of human milk. Human milk amylase could thus contribute to the breast-fed infant's ability to digest starch.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.