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.

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.

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.

Instant 99mTc-Labelled Glucoheptonate Kit for Kidney Imaging

1983 ◽  
Vol 22 (05) ◽  
pp. 246-250 ◽  
Author(s):  
M. Al-Hilli ◽  
H. M. A. Karim ◽  
M. H. S. Al-Hissoni ◽  
M. N. Jassim ◽  
N. H. Agha
Keyword(s):  
Sodium Hydroxide Solution ◽  
Normal Subjects ◽  
Organ Distribution ◽  
Stable Complex ◽  
Scintillation Camera ◽  
Ph Adjustment ◽  
The Mean ◽  
The Stability ◽  
Kidney Imaging ◽  
Mean Concentration

Gelchromatography column scanning has been used to study the fractions of reduced hydrolyzed 99mTc, 99mTc-pertechnetate and 99mTc-chelate in a 99mTc-glucoheptonate (GH) preparation. A stable high labelling yield of 99mTc-GH complex in the radiopharmaceutical has been obtained with a concentration of 40-50 mg of glucoheptonic acid-calcium salt and not less than 0.45 mg of SnCl2 2 H2O at an optimal pH between 6.5 and 7.0. The stability of the complex has been found significantly affected when sodium hydroxide solution was used for the pH adjustment. However, an alternative procedure for final pH adjustment of the preparation has been investigated providing a stable complex for the usual period of time prior to the injection. The organ distribution and the blood clearance data of 99mTc-GH in rabbits were relatively similar to those reported earlier. The mean concentration of the radiopharmaceutical in both kidneys has been studied in normal subjects for one hour with a scintillation camera and the results were satisfactory.

Immunologic Assessment of Patients Treated with Bovine Fibrin as a Hemostatic Agent

1996 ◽  
Vol 76 (06) ◽  
pp. 0925-0931 ◽  
Author(s):  
John F Carroll ◽  
Keith A Moskowitz ◽  
Niloo M Edwards ◽  
Thomas J Hickey ◽  
Eric A Rose ◽  
...  
Keyword(s):  
Coagulation Factors ◽  
Allergic Reactions ◽  
Factor V ◽  
Normal Range ◽  
Serum Samples ◽  
Human Fibrinogen ◽  
Bovine Thrombin ◽  
Thrombotic Complications ◽  
The Mean ◽  
Clinically Significant

SummaryTwenty-one cardiothoracic surgical patients have been treated with fibrin as a topical hemostatic/sealing agent, prepared from bovine fibrinogen clotted with bovine thrombin. Serum samples have been collected before treatment with fibrin and postoperatively between 1 and 9 days, 3 and 12 weeks, and 6 and 8 months. The titers of anti-bovine fibrinogen antibodies, measured by ELISA specific for immunoglobulins IgG or IgM, increased to maximal values after about 8 or 6 weeks, respectively. After 8 months, IgG titers were on average 20-fold lower than the mean maximal value, while IgM titers returned to the normal range. IgG was the predominant anti-bovine fibrinogen immunoglobulin as documented by ELISA, affinity chromatography and electrophoresis. Anti-bovine fibrinogen antibodies present in patients reacted readily with bovine fibrinogen, but did not cross-react with human fibrinogen as measured by ELISA or by immunoelectrophoresis. A significant amount of antibodies against bovine thrombin and factor V has been found, many cross-reacting with the human counterparts. No hemorrhagic or thrombotic complications, or clinically significant allergic reactions, occurred in any patient, in spite of antibody presence against some bovine and human coagulation factors. The treatment of patients with bovine fibrin, without induction of immunologic response against human fibrinogen, appeared to be an effective topical hemostatic/sealing measure.

SKIN-FOLD THICKNESS IN NORMAL SUBJECTS AND IN PATIENTS WITH ACROMEGALY AND CUSHING'S SYNDROME

1969 ◽  
Vol 60 (4) ◽  
pp. 705-711 ◽  
Author(s):  
A. D. Wright ◽  
G. F. Joplin
Keyword(s):  
Cushing’S Syndrome ◽  
Normal Subjects ◽  
Cushing's Syndrome ◽  
Normal Range ◽  
Clinical Method ◽  
Skin Fold Thickness ◽  
Skin Fold ◽  
Normal Mean ◽  
The Mean ◽  
Age And Sex

ABSTRACT A simple clinical method of determining the skin-fold thickness on the dorsum of the hand has been described using the Harpendon spring-loaded caliper. A normal range for age and sex has been established in 258 normal subjects. The mean skin-fold thickness was greater in men than in women, and in both decreased with age, falling from 2.85 to 1.75 mm in men, and from 2.65 to 1.60 mm in women (aged 15–20 to 70–80). In 48 acromegalic patients, 71 % of the skin-fold measurements were abnormally thick. In 12 patients with Cushing's syndrome, although all measurements were below the normal mean, 42 % only were abnormally thin.

The Influence of Acenocumarole on the Fibrinogen-turnover in Normal Subjects, Venous Thrombosis and Congestive Heart Failure

1972 ◽  
Vol 28 (03) ◽  
pp. 496-508
Author(s):  
A. P. C. van der Maas ◽  
F. A. G Teulings ◽  
W Schopman ◽  
G. J. H. den Ottolander
Keyword(s):  
Heart Failure ◽  
Congestive Heart Failure ◽  
Venous Thrombosis ◽  
Anticoagulant Therapy ◽  
Normal Subjects ◽  
Time Interval ◽  
Normal Range ◽  
The Mean ◽  
The Moment ◽  
Continuous Deposition

SummaryUsing 131Iodine-tagged fibrinogen the influence of acenocumarole on the biological half-life of fibrinogen was investigated in healthy patients, patients with venous thrombosis and patients with congestive heart failure.In 16 healthy patients the mean t½ was 3.8 days. In two of them after administration of acenocumarole the t½ was lengthened. This supports the opinion of a continuous deposition of fibrin on the vascular endothelium in the hemostatic balance.In 13 patients with venous thrombosis the mean t½ was 2.45 days, lengthening to the normal range after acenocumarole therapy. The time interval between the start of acenocumarole therapy and the moment of normalization of the t½ was approximately 4 days. The prothrombin time-index at this moment was 2.3 (thrombotest 5%), which argues in favour of a vigorous anticoagulant therapy.In our 10 patients with congestive heart failure probably venous thrombosis occurred in 40%. Prophylactic anticoagulant therapy as in surgical patients therefore has to be considered.

Redefinition of the Normal Range for Serum Sodium

1968 ◽  
Vol 14 (2) ◽  
pp. 172-178 ◽  
Author(s):  
R B Payne ◽  
M J Levell
Keyword(s):  
Serum Sodium ◽  
Normal Subjects ◽  
Sodium Concentration ◽  
Normal Serum ◽  
Hospital Environment ◽  
Serum Urea ◽  
Water Metabolism ◽  
Normal Range ◽  
The Mean ◽  
A Prospective Study

Abstract The serum sodium concentrations of three groups of patients selected from laboratory records and of one group of outpatients selected for a prospective study were examined. The mean serum sodium concentration of inpatients with normal serum urea concentrations was 8.5 mEq./ L. lower than that of a group of healthy normal subjects. Part of this difference (2.6 mEq./L.) could be attributed to a nonspecific effect of illness. It was not possible to demonstrate any effect due to the hospital environment, but the results do not exclude the possibility of such an effect. It was concluded that all or most of the remaining difference was due to weighting of the inpatient data by low values of pathologic significance; the proportion of these low values was too great to allow a normal range to be extracted from the data by statistical methods. The concept of the normal range is discussed. It is suggested that two ranges are required for serum sodium, a normal range (137-147 mEq./L. in this laboratory) to make assertions about alterations in specific diseases, and a range derived from patients likely to have no manifest disturbances of salt and water metabolism (135-144 mEq./ L.) to detect such disturbances.

Sandwich enzyme immunoassay of osteocalcin in serum with use of an antibody against human osteocalcin

1993 ◽  
Vol 39 (6) ◽  
pp. 942-947 ◽  
Author(s):  
D A Monaghan ◽  
M J Power ◽  
P F Fottrell
Keyword(s):  
Monoclonal Antibody ◽  
Enzyme Immunoassay ◽  
Solid Phase ◽  
Sandwich Elisa ◽  
Normal Subjects ◽  
Enzyme Linked Immunosorbent Assay ◽  
Serum Samples ◽  
Standard Curve ◽  
Microtiter Plates ◽  
Human Osteocalcin

Abstract We have developed and thoroughly validated a solid-phase sandwich enzyme-linked immunosorbent assay (ELISA) on microtiter plates for osteocalcin in human serum with use of an antibody raised against human osteocalcin. We used a monoclonal antibody against bovine osteocalcin as the capture antibody; the second antibody was a polyclonal antibody against human osteocalcin. The amount of bound second antibody was determined with use of swine anti-rabbit antibody labeled with horseradish peroxidase. We demonstrated independence of volume and determined the recovery of added standard and within- and between-assay precision. The minimal detection limit for osteocalcin was between 1.0 and 1.5 micrograms/L and the midpoint of the standard curve ranged from 14 to 17 micrograms/L. The intraassay CV was < or = 8% in the range 2.7-52 micrograms/L; the interassay CV was usually < or = 15% in the same range. Analytical recovery of human osteocalcin standard added to serum samples was consistently > 90%. Values for osteocalcin measured in serum from 44 normal subjects were similar to those obtained with a competitive enzyme immunoassay (EIA) that used a monoclonal antibody against bovine osteocalcin. There was a good correlation between the two assays [r2 = 0.877, slope and intercept (+/- SE) = 0.88(+/- 0.051) and 0.316(+/- 0.523), respectively]. The range and mean (+/- SD) for the sandwich ELISA and the competitive EIA were 1.7-18.1 micrograms/L [8.7(+/- 4.4) micrograms/L] and 1.9-22.8 micrograms/L [9.1(+/- 4.4) micrograms/L], respectively.

Immunoradiometric assay of human intact proinsulin applied to patients with type 2 diabetes, impaired glucose tolerance, and hyperandrogenism

1994 ◽  
Vol 40 (5) ◽  
pp. 754-757 ◽  
Author(s):  
D Chevenne ◽  
J Ruiz ◽  
L Lohmann ◽  
A Laudat ◽  
H Leblanc ◽  
...  
Keyword(s):  
Type 2 Diabetes ◽  
Monoclonal Antibody ◽  
Detection Limit ◽  
Glucose Tolerance ◽  
Impaired Glucose Tolerance ◽  
Immunoradiometric Assay ◽  
Serum Samples ◽  
The Mean

Abstract We describe an immunoradiometric assay for human intact proinsulin in serum. In this method, one monoclonal antibody, coated onto polyacrylamide beads, cross-reacts with proinsulins and insulin. A sandwich is formed with intact proinsulin, split (65-66) proinsulin, and des (64-65) proinsulin binding with an 125I-labeled monoclonal antibody specific for an epitope at the intact B-C junction of proinsulin. Because split (65-66) and des (64-65) proinsulin concentrations are very low in serum, this assay essentially measures intact proinsulin. When we used 1-mL serum samples, the mean detection limit was 0.4 pmol/L. Mean proinsulin concentrations (pmol/L) were 3.4 (range 1-9.1) in healthy fasting subjects, 28.5 (9.7-101) in patients with type 2 diabetes (treated with metformin and sulfonylureas), 5.0 (1.6-9.3) in women with hyperandrogenism and normal insulinemia, 10.3 (2.6-36) in women with hyperandrogenism and hyperinsulinemia, and 8.5 (4.8-21.3) in patients with impaired glucose tolerance.

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.

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