Renal clearance of pancreatic and salivary amylase relative to creatinine clearance in patients with renal disease and proteinuria.

1988 ◽  
Vol 34 (3) ◽  
pp. 589-591 ◽  
Author(s):  
J F Wetzels ◽  
J C Hafkenscheid ◽  
M Hessels ◽  
A J Hoitsma ◽  
R A Koene
Keyword(s):  
Renal Disease ◽  
Creatinine Clearance ◽  
Fractional Excretion ◽  
Relative Increase ◽  
Pancreatic Amylase ◽  
Salivary Amylase ◽  
Fractional Clearance ◽  
The Mean ◽  
Beta 2 Microglobulin ◽  
Amylase Isoenzymes

Abstract To study the charge-selective properties of the glomerular filter in renal disease, we measured the fractional clearance, relative to creatinine clearance (ECC), of the amylase isoenzymes pancreatic amylase and salivary amylase, which have identical size but different charge. In 63 healthy subjects the mean (and SD) fractional excretion of pancreatic amylase, 4.07% (1.24%), was fourfold that of salivary amylase: 1.02% (0.54%). For 29 patients with renal disease and proteinuria, the mean fractional excretion of pancreatic amylase was significantly lower, 3.31% (1.94%), and that of salivary amylase significantly higher, 2.06% (1.41%), than in controls. In these patients, fractional excretions of both these isoenzymes were negatively correlated with urinary excretion of beta 2-microglobulin and ECC. Evidently, differences in clearances of pancreatic and salivary amylase are a consequence of differences in charge-related glomerular filtration. The relative increase of salivary amylase clearance in patients with renal disease and proteinuria is most probably caused by a loss of the charge-selective properties of the glomerular basement membrane.

Specific immunoassay of alpha-amylase isoenzymes in human serum.

1985 ◽  
Vol 31 (8) ◽  
pp. 1331-1334 ◽  
Author(s):  
M Gerber ◽  
K Naujoks ◽  
H Lenz ◽  
W Gerhardt ◽  
K Wulff
Keyword(s):  
Monoclonal Antibody ◽  
Human Serum ◽  
Enzyme Immunoassay ◽  
Amylase Activity ◽  
Alpha Amylase ◽  
Pancreatic Amylase ◽  
Routine Method ◽  
Salivary Amylase ◽  
Amylase Isoenzymes

Abstract A monoclonal antibody (66C7) was prepared that specifically binds human salivary amylase (EC 3.2.1.1); it cross reacts with human pancreatic amylase by less than 1%. Two procedures are described for determination of isoamylases in human serum with this antibody: an enzyme immunoassay for determining amylase of salivary origin, and a routine method in which this amylase is immunoprecipitated and the remaining (pancreatic) amylase activity is assayed. Results by the two methods correlate well.

Automated measurement of amylase isoenzymes with 4-nitrophenyl-maltoheptaoside as substrate and use of a selective amylase inhibitor.

1984 ◽  
Vol 30 (7) ◽  
pp. 1219-1222 ◽  
Author(s):  
H Okabe ◽  
Y Uji ◽  
K Netsu ◽  
A Noma
Keyword(s):  
Standard Method ◽  
Selective Inhibitor ◽  
Pancreatic Amylase ◽  
Automated Measurement ◽  
Salivary Amylase ◽  
Amylase Inhibitor ◽  
Amylase Isoenzymes ◽  
Method R ◽  
Serum And Urine ◽  
Serum And Urine Samples

Abstract We automated a kinetic procedure for determining amylase isoenzymes in serum and urine samples. We used 4-nitro-phenylmaltoheptaoside as substrate and a selective amylase inhibitor with the Abbott-VP bichromatic system. By use of the maximum differences between pancreatic (P) and salivary (S) amylase activities remaining after inhibition by the selective inhibitor and by use of the linear range, a one-point standard method for calibration is proposed for determining amylase activities between about 50 and 1500 U/L when the P/S ratio exceeds 0.2. Results correlated well with those by electrophoresis and the Phadebas method (r = 0.99 for both pancreatic and salivary amylase). Reproducibilities (CVs) were 1.5% to 5.5% for pancreatic amylase and 1.4% to 3.3% for salivary amylase in serum, 0.8% to 2.0% for pancreatic amylase and 0.8% to 2.3% for salivary amylase in urine.

Catalytic concentrations of amylase isoenzymes: an assay with wheat-germ inhibitor and 4-nitrophenylmaltopentaoside plus 4-nitrophenylmaltohexaoside as substrate.

1986 ◽  
Vol 32 (8) ◽  
pp. 1577-1580
Author(s):  
A Jiménez ◽  
J Arenas ◽  
I Santos ◽  
A Martínez
Keyword(s):  
Biological Samples ◽  
Wheat Germ ◽  
Selective Inhibitor ◽  
Pancreatic Amylase ◽  
Inhibition Rate ◽  
Salivary Amylase ◽  
Manual Method ◽  
Amylase Inhibitor ◽  
Amylase Isoenzymes

Abstract We coupled a kinetic procedure to a selective inhibiting method for determining amylase isoenzymes in biological samples, using 4-nitrophenylmaltopentaoside plus 4-nitrophenylmaltohexaoside as substrate and a wheat-germ selective inhibitor with the Gilford S-III spectrophotometer. On plotting remaining amylase activities/total amylase activities (R/T) vs pancreatic amylase activities/salivary amylase activities (P/S) ratios, we found the curve to be linear for P/S ratios from 0.2 to 5. The inhibition rate of amylase inhibitor was constant in solutions having total amylase activities between 20 and (at least) 900 U/L. CVs were 3.1 to 7.1% for pancreatic amylase and 2.0 to 12.9% for salivary amylase in serum. Correlation with the Phadebas method was excellent (r = 0.99) for both pancreatic and salivary amylase. We also automated this procedure in an Hitachi 705 analyzer and correlated the results (r = 0.99) with those by our manual method.

scholarly journals Radioimmunoassay of Human Pancreatic Amylase with Monoclonal Antibody

1989 ◽  
Vol 26 (5) ◽  
pp. 416-421 ◽  
Author(s):  
Chiyo Fujita ◽  
Chihiro Kasai ◽  
Hiromi Kosuge ◽  
Kenji Ogata ◽  
Ichiyo Oshima ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Acute Pancreatitis ◽  
Normal Subjects ◽  
Enzymic Activity ◽  
Pancreatic Amylase ◽  
Normal Range ◽  
Salivary Amylase ◽  
Serum Samples ◽  
The Mean ◽  
Mean Concentration

A monoclonal antibody (E-21) was obtained that specifically binds to human pancreatic amylase and shows negligible cross-reaction with human salivary amylase. Using this antibody a radioimmunoassay was developed for pancreatic amylase in human serum. The assay was shown to be sensitive (detectable up to 7 mg/L), reproducible, and specific for pancreatic amylase. In normal subjects, the mean concentration of serum pancreatic amylase determined by this method was 36·3 mg/L with a 95% confidence range of 16·5 to 79·2 mg/L. A good correlation was observed between the concentrations of immunoreactive pancreatic amylase (IR-PA) and enzymatic activities in 20 serum samples ( r = 0·97). The concentration of serum IR-PA was below the detectable limit in pancreatectomised patients, and was greatly increased in patients with acute pancreatitis; the latter was accompanied by parallel changes in total enzymic activity. In patients with mumps, the serum IR-PA level was within the normal range whereas the total enzymic activity was elevated.

Human amylase isoenzymes separated on concanavalin A--Sepharose.

1979 ◽  
Vol 25 (8) ◽  
pp. 1406-1410 ◽  
Author(s):  
T Takeuchi
Keyword(s):  
Concanavalin A ◽  
Serum Amylase ◽  
Sodium Dodecyl ◽  
Relative Molecular Mass ◽  
Pancreatic Amylase ◽  
Major Peak ◽  
Salivary Amylase ◽  
Isoelectric Points ◽  
Minor Peak ◽  
Amylase Isoenzymes

Abstract Human salivary amylase and pancreatic amylase were purified and characterized. These amylases gave two bands and one band, respectively, each staining for both protein and sugar, after electrophoresis on sodium dodecyl sulfate--polyacrylamide gel. The relative molecular mass (Mr) or pancreatic amylase was calculated to be 60 000; for the two components (A and B) of salivary amylase the Mr were 61 000 and 64 000. The two salivary amylases were separated by chromatography on concanavalin A--Sepharose; only component B bound to concanavalin A. The carbohydrate content of pancreatic amylase was 1.61 +/- 1.02% (SD), and of salivary amylases A and B 2. 18 +/- 0.71% and 8.77 +/- 2.28%, respectively. The salivary and pancreatic amylases had completely identical antigenicities against antibody to either. On isoelectric focusing, pancreatic amylase showed one peak at pH 7.0, salivary amylase A showed a major peak at pH 6.4 WITH A TRACE OF MATERIAL At pH 5.9, and salivary amylase B a major peak at pH 5.9 and one minor peak at pH 6.4. Serum amylase was separated into two major peaks with isoelectric points (pl) of 6.4 and 7.0, respectively, and one minor peak, with a pl of 5.9. Only a small part of the serum amylase with a pl of 5.9 combined with concanavalin A; the two other serum amylases did not.

Three methods compared for determination of pancreatic and salivary amylase activity in serum of cystic fibrosis patients.

1986 ◽  
Vol 32 (2) ◽  
pp. 296-300 ◽  
Author(s):  
R O Wolf ◽  
V S Hubbard ◽  
B K Gillard ◽  
A Kingman
Keyword(s):  
Cystic Fibrosis ◽  
Gel Electrophoresis ◽  
Serum Amylase ◽  
Amylase Activity ◽  
Pancreatic Insufficiency ◽  
Polyacrylamide Gel Electrophoresis ◽  
Pancreatic Amylase ◽  
Salivary Amylase ◽  
Amylase Isoenzymes

Abstract We evaluated three methods for serum amylase (EC 3.2.1.1) isoenzymes to determine whether they are interchangeable and to test their ability to discriminate between cystic fibrosis patients with and without pancreatic insufficiency. One method involved salivary amylase inhibitor (O), and two were polyacrylamide gel electrophoresis separations differing in method of detection--either direct zymogram (G) or gel slicing followed by activity estimates per slice (W). Results for percentage pancreatic amylase differed significantly. Reproducibility for percentage pancreatic amylase was high, moderate, and low (r = 0.95, 0.53, and 0.02) for methods G, O, and W, respectively; moderate (r = 0.60) among the three methods; and moderate between pairs. Therefore, this result for a subject must be considered relative to the method used in its determination. The clinical diagnosis of pancreatic insufficiency was verified by 77.8%, 83.3%, and 94.4% correct classification rates for methods O, W, and G, respectively. Evidently, method G is the most efficient and may be the method of choice for measuring serum amylase isoenzymes in cystic fibrosis.

Simultaneous Iothalamate, Creatinine, and Urea Clearances in Children With Renal Disease

PEDIATRICS ◽  
1977 ◽  
Vol 59 (2) ◽  
pp. 219-223 ◽  
Author(s):  
Ben H. Brouhard ◽  
Luther B. Travis ◽  
Robert J. Cunningham ◽  
Michael Berger ◽  
Hugo F. Carvajal
Keyword(s):  
Glomerular Filtration Rate ◽  
Renal Disease ◽  
Creatinine Clearance ◽  
Glomerular Filtration ◽  
Filtration Rate ◽  
Clinical Tool ◽  
The Mean ◽  
Low Levels

Glomerular filtration rate (GFR) is often used to evaluate and manage patients with renal disease. Few studies in children have compared accurate estimations of GFR (clearance of inulin and/or iothalamate) with the clearance of creatinine which, because of simplicity, has been used as an approximation of GFR. At reduced levels of GFR, studies in adults suggest that the mean of the creatinine and urea clearances closely approximate the GFR. The present investigation shows that the clearance of creatinine approximates the GFR at normal levels; however, at reduced levels the creatinine clearance and the mean of the creatinine and urea clearances both overestimate the GFR as measured by iothalamate. The clearance of creatinine remains a useful clinical tool if its limitations at low levels of GFR are realized.

Interaction of immobilized anti-salivary amylase antibody with human macroamylases: implications for use in a pancreatic amylase assay to distinguish macroamylasemia from acute pancreatitis.

1989 ◽  
Vol 35 (8) ◽  
pp. 1651-1654
Author(s):  
T E Mifflin ◽  
R W Forsman ◽  
D E Bruns
Keyword(s):  
Acute Pancreatitis ◽  
Healthy Volunteers ◽  
Amylase Activity ◽  
Electrophoretic Analysis ◽  
Pancreatic Amylase ◽  
Salivary Amylase ◽  
Isoenzyme Composition ◽  
The Mean

Abstract We examined the ability of an immobilized antibody to salivary amylase (Clin Chem 1985;33:1283-8) to react with amylase in macroamylasemic sera. The antibody removed 50% (SD 23%) of the total amylase activity from 39 macroamylase sera, a percentage indistinguishable (P greater than 0.75) from the percentage removed from concurrently analyzed sera from healthy volunteers (49%, SD 11%). Electrophoretic analysis of 23 macroamylasemic sera revealed that the antibody removed only part of the macroamylase band(s) in 71% of the cases. We conclude that the mean isoenzyme composition of the macroamylase complexes is essentially identical to the mean isoenzyme distribution in normal sera (i.e., about half salivary and half pancreatic amylase). Further, the immobilized antibody can be used to distinguish most patients with macroamylasemia from those with acute pancreatitis, because sera from the latter contain an increased proportion (greater than 80%) of pancreatic amylase.

scholarly journals Renal Involvement in Children with Type 2 Diabetes Mellitus Onset: A Pilot Study

Children ◽  
2021 ◽  
Vol 8 (8) ◽  
pp. 627
Author(s):  
Pierluigi Marzuillo ◽  
Anna Di Sessa ◽  
Pier Luigi Palma ◽  
Giuseppina Rosaria Umano ◽  
Cesare Polito ◽  
...  
Keyword(s):  
Diabetes Mellitus ◽  
Type 2 Diabetes ◽  
Type 2 Diabetes Mellitus ◽  
Renal Involvement ◽  
Kidney Injury ◽  
Fractional Excretion ◽  
Tubular Damage ◽  
Beta 2 ◽  
Beta 2 Microglobulin

Type 2 Diabetes Mellitus (T2DM) is a main cause of chronic kidney disease (CKD) in adulthood. No studies have examined the occurrence of acute kidney injury (AKI)—that enhances the risk of later CKD—and renal tubular damage (RTD)—that can evolve to AKI—in children with onset of T2DM. We aimed to evaluate the prevalence and possible features of AKI and RTD in a prospectively enrolled population of children with onset of T2DM. We consecutively enrolled 10 children aged 12.9 ± 2.3 years with newly diagnosed T2DM. AKI was defined according to the KDIGO criteria. RTD was defined by abnormal urinary beta-2-microglobulin and/or tubular reabsorption of phosphate (TRP) < 85% and/or fractional excretion of Na > 2%. None of the patients developed AKI, whereas 3/10 developed RTD with high beta-2-microglobulin levels (range: 0.6–1.06 mg/L). One of these three patients also presented with reduced TRP levels (TRP = 70%). Proteinuria was observed in two out of three patients with RTD, while none of patients without RTD had proteinuria. Patients with RTD presented higher beta-2-microglobulin, acute creatinine/estimated basal creatinine ratio, and serum ketones levels compared with patients without RTD. In conclusion, in our pilot observation, we found that none of the 10 children with T2DM onset developed AKI, whereas three of them developed RTD.

Isolation and Measurement of Pancreatic Amylase in Human Serum and Urine

1972 ◽  
Vol 18 (12) ◽  
pp. 1493-1497 ◽  
Author(s):  
L Fridhandler ◽  
J Edward Berk ◽  
M Ueda
Keyword(s):  
Acute Pancreatitis ◽  
Human Serum ◽  
Fallopian Tube ◽  
Normal Subjects ◽  
Pancreatic Amylase ◽  
Salivary Amylase ◽  
Tissue Homogenates ◽  
Quantitative Procedure ◽  
Lines Of Evidence ◽  
Serum And Urine

Abstract We describe a sensitive quantitative procedure for separating isoamylases in human serum, urine, and tissue homogenates. Two components have been discerned with chromatographic characteristics resembling those of pancreatic and salivary amylases, respectively. Several lines of evidence—derived from studies in normal subjects, pancreatectomized patients, and patients with acute pancreatitis—indicate that the pancreas is probably the source of the component in serum and urine that exhibits characteristics of pancreatic amylase. The source of the component resembling salivary amylase has not yet been fully defined. Isoamylase analysis of extracts of fallopian tube and liver revealed two amylase components with chromatographic properties similar to pancreatic and salivary amylases, respectively.

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