Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.1.3.1 (alkaline phosphatase)
47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The suitability of thirteen commercially available control sera for measuring alkaline phosphatase (EC 3.1.3.1; orthophosphoric acid monoester phosphohydrolase, ALP) activity in human serum was tested. Apart from differences in ALP activity observed in some reconstituted commercial sera, the behaviour of control materials towards experimental variables such as the nature and concentration of the substrate, pH and type of buffer (or PO4-acceptor) together with the composition of the isoenzymes present in human serum highlights the problems and difficulties if commercial materials are to be used as control sera. The half-saturation constants in control sera were in all cases smaller than those of ALP isoenzymes from bone and liver. The shape of substrate activity curves and the pH optimum in most of control sera differed from that of human serum. The discrepant kinetic data of control materials and human serum may mask or suggest changes relevant to commercial quality control serum but not to samples of human serum.
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PMID:Suitability of commercial control sera for the quality control of activity determination of alkaline phosphatase. 3 93

Human placenta alkaline phosphatase (HP-ALP), a glycoprotein, was stained histochemically for the purpose of examining the concanavalin A (Con A) binding sites on the cell surface. HP-ALP was bound to the cell surface by Con A. This simple method successfully detected Con A binding sites on the cell surface.
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PMID:A new histochemical method using human placenta alkaline phosphatase for demonstrating concanavalin A binding sites on cell surfaces. 18 Jul 55

We have studied five patients who have exhibited an unusual alkaline phosphatase isoenzyme (ALP EC 3.1.3.1) migrating in an ultrafast position electrophoretically on cellulose acetate. This ALP isoenzyme has been identified in patients with benign and malignant liver diseases. In addition, a number of these patients exhibited a regular ALP liver isoenzyme and a fast (preliver) ALP isoenzyme in conjunction with the ultrafast ALP liver isoenzyme.
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PMID:Clinical significance of an ultrafast alkaline phosphatase isoenzyme. 53 64

The activities of serum alkaline phosphatase (serum ALP), leucine aminopeptidase (serum LAP), and alanine aminotransferase (serum ALT) were determined in 15 cats before and after treatment by 3 methods: common bile duct occlusion, left hepatic duct(s) occlusion, and carbon tetrachloride administration. Significant increases in serum ALP, LAP, and ALT activities occurred in all cats in the 3 groups. Sustained mean increases of ninefold in ALP and 13-fold in LAP occurred in the cats with common bile duct occlusion. Lesser mean increases of these enzymes (fourfold) occurred in the cats with partial biliary occlusion. Transient mean increases (100-fold) in ALT occurred in the carbon tetrachloride-treated cats. Urine ALP excretion was measured in 3 cats with common bile duct occlusion. There was no significant difference between rates of urine ALP excretion before and after common bile duct occlusion. Specific ALP activities of hepatic extracts from normal cats and biliary-obstructed cats were compared. Mean specific activity was onefold higher in liver from cats with common bile duct occlusion of 21 days' duration. The findings in the present studies were interpreted to indicate that serum ALP and LAP are useful to detect biliary occlusive disease in cats and, in conjunction with serum ALT, may be used to differentiate primary hepatodegenerative disease and biliary occlusive disease.
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PMID:Alkaline phosphatase, leucine aminopeptidase, and alanine aminotransferase activities with obstructive and toxic hepatic disease in cats. 56 Aug 16

Coinciding investigations of the 85Sr test and of bone derived serum alkaline phosphatases activity were undertaken in 38 patinets with locomotor system diseases. In 15 patients there was congruence between the positive result of the 85Sr test and an increased activity of B-ALP. In 5 patients there was congruence between negative outcome of B-ALP and negative 85Sr test. The activities of T-ALP, B-ALP, L-ALP and I-ALP were compared with a group of 124 healthy controls. The causes of 18 incongruent results were analysed. In rhizomelic form of ASp, active Paget's disease, osteomalacia and in some forms of osteoporosis there was congruence between increased activity of B-ALP and the positive 85Sr test over the clinically involved area of the locomotor system. In ankylosing spondylitis (without rhizomelic involvement) there may be a moderate fall of B-ALP activity but the 85Sr test is usually positive; this may correspond with metabolic activity in the paravertebral region of the ligaments. Low B-ALP activity and positive 85Sr test in MP may refer to a latent process in the bone apparatus without marked activity of osteoblasts. The fall of B-ALP may be a result of therapy or due to the reduced capacity of B-ALP to be released from the bone. In osteomalacia the rapid fall of 85Sr activity during the test is the cause by the presence of pathological osteoid which may be, even in patients with hypertension, of renal origin. A method was described permitting the evaluation of the process of active incorporation of bone minerals (after 8 days). The activity of the 85Sr test over clinically silent areas (e.g. spine) may indicate a decompensated process in the spine due to an involvement to the large joints. The two methods used in this study are metabolically different (85Sr binds to proteoglycans and inorganic structures of bone tissue, alkaline phosphatase to the activity of osteoblasts) and prove to be clinically valuable. Detailed analysis of the results makes it possible to define the stages of clinical activity of disease and to check more exactly the efficiency of the therapeutic method.
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PMID:[Clinical evaluation of the results of the Sr85 test and of bone alkaline phosphatase isoenzyme activity]. 87 Oct 69

Serum gamma-glutamyl transferase (GGT) was separated into nine to 11 isoenzyme bands (designated as GGT I-XI) by vertical slab electrophoresis on polyacrylamide gradient gel. The diagnostic value of GGT isoenzyme II (GGT II) for hepatocellular carcinoma (HCC) was studied, and the results were as follows: 1) GGT II was positive in 90% of 90 cases of HCC, and negative in most patients with acute and chronic viral hepatitis, extrahepatic tumors, in pregnant women, and in healthy controls; 2) the positive rate of GGT II assay was higher than that of alkaline phosphatase isoenzyme I (ALP I), alpha-fetoprotein (AFP), and alpha 1-antitrypsin (AAT) in 101 cases of HCC. In cases in which the AFP was greater than 50 ng/ml or less than 50 ng/ml, the positive rates of GGT II were 70.8% and 75-100%, respectively; 3) of 14 cases of small-size HCC, the positive rate of GGT II was 78.6%, which was higher than that of AFP (50%), AAT (28.6%), and ALP I (0%); 4) of 62 cases that were false-positive for GGT II assay, 24.2% developed into HCC during a follow-up of 2.1-20 months. In subjects with persistent and recurrent positivity of GGT II, 86.7% and 22.2%, respectively, developed HCC. No patient with temporal positivity of GGT II developed HCC. The results show that GGT II can be applied as an additional marker for HCC, and is valuable not only for the diagnosis of clinical HCC, but for the detection of small or subclinical HCC. Periodic follow-up with assay of GGT II in patients at high risk for HCC may predict the development of hepatoma.
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PMID:Diagnostic value of serum gamma-glutamyl transferase isoenzyme for hepatocellular carcinoma: a 10-year study. 135 62

Twenty-two patients with clinical, biochemical, immunological and pathological characteristics compatible with primary biliary cirrhosis were studied. There were 17 women and 5 men with a mean age of 57.4 +/- 15.2 years and a mean follow-up of 24.1 +/- 20.1 months. Four of them expired during the follow-up and eighteen patients now survive. The most common complaints were fatigue (63.6%) and itching (59.1%). Only one case (4.5%) was asymptomatic in this series. The major physical findings were jaundice (50%) and hepatomegaly (50%). The significant laboratory findings were: elevation of alkaline phosphatase (91% of the cases greater than 3 times the upper limit of normal), gamma-glutamyl transpeptidase (100% of the cases greater than 4 times the upper limit of normal), aspartate transaminase (95%) and alanine transaminase (100%), presence of anti-mitochondrial antibodies (91%), antinuclear antibodies (73%) and the elevation of IgM (88%). One case was associated with ulcerative colitis. Pathological staging in this series revealed 57.9% of stage II, 26% of stage III, 10% of stage IV and 5.3% of stage I. All patients with granuloma survived but 4 of the 5 patients with cholestasis died during follow-up. The results show that the features in this series of PBC were similar to those observed in western countries. The very high ALP and gamma-GT level as well as only one asymptomatic case in this series, suggest that our patients were diagnosed at a late stage. The reason(s) for the higher positivity of ANA, particularly the speckled type and a lower rate of associated auto-immune disease requires further study. Liver biopsy in predicting a prognosis is valuable.
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PMID:[A clinicopathological study in primary biliary cirrhosis]. 135 58

We evaluated N-methyl-D-glucamine (MEG) as a buffer for assay of alkaline phosphatase (ALP; EC 3.1.3.1) and compared the MEG-based assay with the current International Federation of Clinical Chemistry Reference Method for ALP (IFCC/RM/ALP), in which 2-amino-2-methyl-1-propanol (AMP) is the pH buffer. The ALP assay in MEG at 30 and 37 degrees C shows excellent correlation with the IFCC/RM/ALP at 30 degrees C, but yields proportionately higher ALP activities (8.2% at 30 degrees C and 57% at 37 degrees C). ALP is unstable in both MEG and AMP at 37 degrees C. Serum incubated in MEG undergoes a pH-dependent biphasic loss of ALP activity: an initial rapid 5% loss after 1 min of incubation and a 10% loss per hour thereafter. A similar pattern was seen for incubation with AMP. The use of a serum-initiated reaction (no preincubation of enzyme with buffer) eliminated the early loss in activity. The addition of the metal ion buffer N-hydroxyethylethylenediaminetriacetic acid, along with low concentrations of Zn and Mg, as used in the IFCC/RM/ALP, reduced the slow loss in activity over time, as did decreasing the reaction temperature to 30 degrees C, but had no effect on the early rapid decay in activity seen in the first minute. Moderate transphosphorylation (45%) and nonenzymatic hydrolysis (3.3 U/L) were observed with MEG under the conditions of the assay (37 degrees C). A comparison of different lots of MEG from two manufacturers showed no significant difference in ALP activities.
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PMID:Investigation of N-methyl-D-glucamine buffer for assay of alkaline phosphatase in serum. 142 26

Hypophosphatasia is an inherited disorder characterized by defective mineralization of the skeletal and dental structures of the body and deficient liver/bone/kidney alkaline phosphatase (L/B/K ALP) activity. There has been a tremendous advance in our knowledge of this condition over the last decade due to the advent of highly specific DNA probes and novel microanalytic techniques. The purpose of this paper is threefold: to review the dental aspects of current literature about this rare condition; to present a case (and family study) that was diagnosed in a 5-yr-old boy from 0.14 microliters of gingival crevicular fluid, using a new ultrasensitive chemiluminescent assay for the enzyme alkaline phosphatase; and to provide strong evidence for an autosomal dominant mode of inheritance.
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PMID:Hypophosphatasia: a family study involving a case diagnosed from gingival crevicular fluid. 143 39

The renal toxicity of harman and norharman, administered for 2 or 4 weeks at dietary levels of 1,000, 500, or 0 parts per million (ppm), was investigated in 6-week-old male F344/DuCrj rats. Although rats fed 1,000 ppm harman or norharman, but not the 500 ppm level, demonstrated marked body weight retardation from 1 week to termination, no mortalities occurred. Marked elevation of water consumption was evident in rats given harman or norharman at 1,000 ppm, but not at 500 ppm, together with large increases in urine of low specific gravity. Urinary lysosomal enzymes (N-acetyl-beta-D-glucosaminidase, NAG, and lactate dehydrogenase, LDH) and sugar levels were increased, and the brush border enzymes (gamma-glutamyl transpeptidase, GGT, and alkaline phosphatase, ALP) decreased. Furthermore, serum biochemistry revealed clear elevation of parameters indicating renal toxicity in these rats. Histopathologically, rats fed 1,000 ppm harman or norharman, but not 500 ppm, demonstrated focal toxic renal degenerative/necrotic and regenerative lesions in proximal, distal, and collecting tubules. These changes were associated with a clearly increased labeling index (LI) of the nuclei of renal tubular epithelial cells on immunohistochemical staining for 5-bromo-2'-deoxyuridine (BrdU). Chemical specific crystal formation within tubular lumina was evident in rats fed 1,000 ppm, but not 500 ppm, this being considered the cause of the renal tubular lesions. It was concluded that harman and norharman exert renal toxicity at the dietary level of 1,000 ppm, but not 500 ppm, in male F344 rats.
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PMID:Dose-dependent renal tubular toxicity of harman and norharman in male F344 rats. 147 80


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