Serum Amylase Activity in the Newborn

The presence of measurable quantities of amylase in the serum of newborn infants or in serum derived from cord blood may be demonstrated through the use of a sensitive saccharogenic procedure that permits analysis of small quantities of serum. Serum amylase levels are highly variable during the early part of the neonatal period, but they usually tend to be close to or below the lower limits of normal established for adults. The origins of the serum amylase in the newborn infant remain to be elucidated.

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Total and Free Thyroid Hormone Concentrations in the Neonatal Period

PEDIATRICS ◽

10.1542/peds.53.2.211 ◽

1974 ◽

Vol 53 (2) ◽

pp. 211-216

Author(s):

Allen Erenberg ◽

Dale L. Phelps ◽

Robert Lam ◽

Delbert A. Fisher

Keyword(s):

Thyroid Hormone ◽

Cord Blood ◽

Newborn Infant ◽

Neonatal Period ◽

Hormone Secretion ◽

Newborn Infants ◽

Blood Levels ◽

Free T4 ◽

Free T3 ◽

Serum T3

Radioimmunoassay measurements of serum concentrations of thyroxine (T4), triiodothyronine (T3), free T4 (FT4), free T3 (FT3), and thyroxine binding globulin (TBG) were conducted in full-term newborn infants between birth and 5 days of age. The mean concentrations of T4 and FT4 increased from cord blood levels of 11.9 µg/100 ml and 2.9 ng/100 ml to peak values of 16.2 µg/100 ml and 7 ng/100 ml by 24 to 48 hours of age. Mean serum total and free T3 concentrations increased from cord blood levels of 50.5 ng/100 ml and 146 pg/100 ml to peak values of 419 ng/100 ml and 1,260 pg/100 ml by 24 hours of age. Mean T3/T4 and FT3/FT4 ratios increased from 1/238 to 1/39 and from 1/20 to 1/6, respectively, during this period. By 72 to 126 hours, both the T4 and T3 concentrations had fallen somewhat. Mean serum TBG concentrations were unchanged and approximated 5.0 mg/100 ml during the first 5 days of life. These data confirm earlier reports that the normal newborn infant rapidly becomes chemically hyperthyroid in the neonatal period due to increased thyroid hormone secretion; this neonatal hyperthyroid state is due more to T3 than to T4. The data also confirm earlier reports that the fetus is T3 deficient due to a decreased capacity to monodeiodinate T4 to T3 in extrathyroidal tissues. The rapid increase in serum T3 after delivery at a time when the capacity to convert T4 to T3 is reduced suggests that the increment in serum T3 is due, predominantly, to increased T3 secretion from the thyroid gland stimulated by the neonatal TSH surge. Thus with parturition, the newborn infant is transformed from a state of chemical T3 deficiency to a state of chemical T3 thyrotoxicosis.

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Oxygen Consumption in Platelets of Newborn Infants before and after Stimulation by Thrombin.

Thrombosis and Haemostasis ◽

10.1055/s-0038-1647969 ◽

1976 ◽

Vol 35 (03) ◽

pp. 712-716 ◽

Cited By ~ 3

Author(s):

D. Del Principe ◽

G Mancuso ◽

A Menichelli ◽

G Maretto ◽

G Sabetta

Keyword(s):

Oxygen Consumption ◽

Cord Blood ◽

Umbilical Cord ◽

Newborn Infant ◽

Umbilical Cord Blood ◽

Newborn Infants ◽

O2 Consumption ◽

Adult Control ◽

Healthy Newborn ◽

Before And After

SummaryThe authors compared the oxygen consumption in platelets from the umbilical cord blood of 36 healthy newborn infants with that of 27 adult subjects, before and after thrombin addition (1.67 U/ml). Oxygen consumption at rest was 6 mμmol/109/min in adult control platelets and 5.26 in newborn infants. The burst in oxygen consumption after thrombin addition was 26.30 mμmol/109/min in adults and 24.90 in infants. Dinitrophenol did not inhibit the burst of O2 consumption in platelets in 8 out of 10 newborn infants, while the same concentration caused a decrease in 9 out of 10 adult subjects. Deoxyglucose inhibited the burst in O2 consumption in newborn infant and adult platelets by about 50%. KCN at the concentration of 10−4 M completely inhibited basal oxygen consumption but did not completely inhibit the burst after thrombin. At the concentration of 10−3 M, it inhibited both basal O2 consumption and the burst in infants and adult subjects.

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An Automated, Saccharogenic Method for Determining Serum Amylase Activity

Clinical Chemistry ◽

10.1093/clinchem/16.12.985 ◽

1970 ◽

Vol 16 (12) ◽

pp. 985-989 ◽

Cited By ~ 12

Author(s):

Wendell R O'Neal ◽

Nathan Gochman

Keyword(s):

Glucose Oxidase ◽

Blood Donors ◽

Serum Amylase ◽

Amylase Activity ◽

Serum Glucose ◽

Normal Range ◽

Reducing Substances ◽

Serum Amylase Activity

Abstract An automated adaptation of the Somogyi saccharogenic determination of serum amylase is described in which conventional AutoAnalyzer modules are used. Adequate sensitivity with short incubation is achieved by incorporating glucose oxidase and catalase in the substrate to destroy serum glucose during incubation. Maltose and other dialyzable oligosaccharides are measured with the alkaline copper-neocuproine reaction. A simultaneous blank run is performed to determine reducing substances other than glucose in serum. Precision studies and correlation with a manual saccharogenic method are presented. The normal range was determined from data for 49 healthy blood donors.

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(Washington University case conference): acute pancreatitis, hyperlipemia, and normal amylase.

Clinical Chemistry ◽

10.1093/clinchem/24.5.815 ◽

1978 ◽

Vol 24 (5) ◽

pp. 815-820 ◽

Cited By ~ 2

Keyword(s):

Acute Pancreatitis ◽

Serum Amylase ◽

Amylase Activity ◽

Normal Serum ◽

Case Conference ◽

Diagnosis And Management ◽

Serum Amylase Activity ◽

Washington University

Abstract This case focuses on the biochemical findings in acute pancreatitis and the role of the laboratory in the diagnosis and management of such patients. It also illustrates a major unappreciated problem in the use of amylase determinations in patients with acute pancreatitis: normal serum amylase activity in the presence of hyperlipemia.

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A New Saccharogenic Micromethod for Measurement of Amylase Activity in Biological Fluids

Clinical Chemistry ◽

10.1093/clinchem/16.4.300 ◽

1970 ◽

Vol 16 (4) ◽

pp. 300-304 ◽

Cited By ~ 5

Author(s):

Klaus Lorentz ◽

Detlef Oltmanns

Keyword(s):

Standard Deviation ◽

Blood Donors ◽

Serum Amylase ◽

Amylase Activity ◽

Biological Fluids ◽

Soluble Starch ◽

Starch Digestion ◽

Triphenyltetrazolium Chloride ◽

Serum Amylase Activity ◽

Apparently Healthy

Abstract To determine serum amylase activity we have quantitatively measured the glucose and maltose hydrolyzed from soluble starch by colorimetrically measuring the reduction of colorless triphenyltetrazolium chloride to a red formazan, which is dissolved in methanol. The method is suitable for use with microsamples of all biological fluids, and is specific for the final products of starch digestion. Values found for sera from 55 apparently healthy blood donors ranged from 0.15 to 1.55 (mean, 0.83; standard deviation, ±0.4) mg of glucose per ml per h, corresponding to 7.5 to 78 Somogyi units.

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Effect of Cadmium Exposure on Serum Amylase Activity in Cadmium Electroplating Workers

Environmental Bioindicators ◽

10.1080/15555270601025758 ◽

2006 ◽

Vol 1 (4) ◽

pp. 260-267 ◽

Cited By ~ 2

Author(s):

R. B. Kalahasthi ◽

Rajmohan Hirehal Raghavendra Rao ◽

Rajan Bagalur Krishna Murthy ◽

M. Karuna Kumar

Keyword(s):

Serum Amylase ◽

Amylase Activity ◽

Cadmium Exposure ◽

Serum Amylase Activity

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Microdetermination of Serum Amylase Activity utilizing the 3, 6-Dinitrophthalic Acid Method of Determining Reducing Sugar

YAKUGAKU ZASSHI ◽

10.1248/yakushi1947.94.1_138 ◽

1974 ◽

Vol 94 (1) ◽

pp. 138-143 ◽

Cited By ~ 3

Author(s):

MASATAKE IWASAKI ◽

MUTSUKO OTA ◽

YOSHITAKA OTANI

Keyword(s):

Serum Amylase ◽

Amylase Activity ◽

Reducing Sugar ◽

Acid Method ◽

Serum Amylase Activity

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Modified Form of the Fibrinogen Bβ Chain (des-Gln Bβ), a Potential Long-Lived Marker of Pancreatitis

Clinical Chemistry ◽

10.1373/clinchem.2007.093179 ◽

2007 ◽

Vol 53 (12) ◽

pp. 2105-2111 ◽

Cited By ~ 9

Author(s):

David Schmidt ◽

Stephen O Brennan

Keyword(s):

Plasma Sample ◽

Serum Amylase ◽

Peptide Mapping ◽

Amylase Activity ◽

Pancreatic Disease ◽

Reversed Phase ◽

Ionization Mass ◽

Carboxypeptidase A ◽

Serum Amylase Activity

Abstract Background: During an investigation of genetic variants of fibrinogen, we observed a novel form of the Bβ chain, with a mass decrease of approximately 128 Da, in one of the controls. The plasma sample originated from an individual who had experienced acute pancreatitis a week earlier but whose serum amylase activity had returned to normal. We investigated the structure of the modified fibrinogen and explored its relationship to pancreatic disease. Method: Fibrinogen was isolated from the plasma of 9 individuals with increased pancreatic amylase activity (114–1826 U/L) and presumed pancreatitis and from 6 control individuals with amylase activities <56 U/L. Fibrinogen (or fibrin) Bβ chains were isolated by reversed-phase HPLC and analyzed directly by electrospray ionization mass spectrometry. Tryptic and CNBr peptide mapping and thrombin treatment pinpointed the location of the 128-Da loss in mass. Results: The acquired fibrinogen Bβ chain modification was attributable to the loss of its C-terminal glutamine residue. Incubating purified fibrinogen with pancreatic carboxypeptidase A (CpA) produced an identical modification. The des-Gln Bβ fibrinogen accounted for >80% of the Bβ chains in 3 of the individuals with increased amylase but only approximately 5% of the Bβ chains in control samples. Conclusion: Pancreatic CpA activity is used as an index of acute pancreatic disease, but given that the circulatory half-lives of fibrinogen and CpA are approximately 4 days and only 2.5 h, respectively, measuring des-Gln Bβ fibrinogen, the in vivo product of CpA activity, could provide clinicians with retrospective evidence of disease.

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