scholarly journals Negative modulation of alkaline phosphatase and creatine kinase by homobrassinolide.

2010 ◽  
Vol 2 (3) ◽  
pp. 258-264
Author(s):  
G. Nirmal Kumar ◽  
S. Lakshmy ◽  
K. Srikumar
2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Kai Saito ◽  
Hitoshi Sugawara ◽  
Tamami Watanabe ◽  
Akira Ishii ◽  
Takahiko Fukuchi

AbstractRisk factors associated with 72-h mortality in patients with extremely high serum aspartate aminotransferase levels (AST; ≥ 3000 U/L) are unknown. This single-centre, retrospective, case-controlled, cross-sectional study obtained data from medical records of adult patients treated at Saitama Medical Center, Japan, from 2005 to 2019. We conducted a multivariate logistic after adjusting for age, sex, height, weight, body mass index, Brinkman Index, vital signs, biochemical values, updated Charlson Comorbidity Index (CCI) score, CCI components, and underlying causes. A logistic regression model with selected validity risks and higher C-statistic for predicting 72-h mortality was established. During the 15-year period, 428 patients (133 non-survivors and 295 survivors [cases and controls by survival < 72 and ≥ 72 h, respectively]) with AST levels ≥ 3000 U/L were identified. The 72-h mortality rate was 133/428 (31.1%). The model used for predicting 72-h mortality through the assessment of alkaline phosphatase, creatine kinase, serum sodium, potassium, and phosphorus levels had a C-statistic value of 0.852 (sensitivity and specificity, 76.6%). The main independent risk factors associated with 72-h mortality among patients with AST levels ≥ 3000 U/L included higher serum values of alkaline phosphatase, creatine kinase, serum sodium, potassium, and phosphorus.


Author(s):  
Anna Nowakowska ◽  
Dorota Kostrzewa-Nowak ◽  
Rafał Buryta ◽  
Robert Nowak

Physical exercise strongly affects human metabolism and causes biochemical changes. This study aimed to investigate the relationship between routine plasma biomarker levels and recovery efficiency in soccer players during an entire competitive match season. The players participating in the study were divided into a midfielder/defender group (seven midfielders and seven defenders) and a goalie/substitute group (six persons—goalkeepers and players with a short cumulative match-time). The fasting capillary blood samples were taken 17–24 h after each competitive match. The blood plasma was used to determine the creatinine, urea, alkaline phosphatase, creatine kinase, lactate dehydrogenase, aspartate and alanine aminotransferase, iron and magnesium levels of the athletes. The levels of (AST) (aspartate aminotransferase), (ALT) (alanine aminotransferase) and (Cr) creatinine were higher in the midfielder/defender group than in the control group, but only AST and Cr significantly varied over time (AST decreased, and Cr increased with time). The (LDH) (lactate dehydrogenase) activity and urea level were significantly lower in the midfielder/defender group than in the goalie/substitute group, and it significantly varied over time (LDH decreased, and urea increased with time). No differences in the (CK) creatine kinase and (ALP) alkaline phosphatase activities between the groups was found, although CK increased significantly with time in the midfielder/defender group (particularly midfielders in the spring round). In midfielders, the AST activity and the iron level were significantly lower in the spring than in the autumn round. On the contrary, ALT, CK, urea and magnesium levels were significantly higher in the spring than in autumn round. A long-term measurement of biochemical parameters in elite soccer players indicated that AST, CK, LDH and creatinine levels, when analyzed together, could constitute a useful set of markers for monitoring recovery periods.


1973 ◽  
Vol 19 (9) ◽  
pp. 1079-1080
Author(s):  
Ted W Fendley ◽  
Jane M Hochholzer ◽  
Christopher S Frings

Abstract We have evaluated the effect of diluting serum with water or NaCl solution (8.5 or 9.0 g/liter) before assaying by a manual method for creatine kinase (EC 2.7.3.2), alkaline phosphatase (EC 3.1.3.1), lactate dehydrogenase (EC 1.1.1.27), and aspartate aminotransferase (EC 2.6.1.1) activity. The t test and the F test show no significant difference in the accuracy and precision of the assays at the 95% confidence level when 100 different samples were compared for each enzyme activity after use of the three diluents.


1980 ◽  
Vol 26 (2) ◽  
pp. 297-300
Author(s):  
K Bauer ◽  
P M Bayer ◽  
E Deutsch ◽  
F Gabl

Abstract We describe a simple method for detecting enzyme--immunoglobulin G (IgG) complexes in human serum. Protein-A Sepharose CL-4B binds IgG and therefore also the enzyme--IgG complexes, which can then be separated easily from the serum by centrifugation. We demonstrate this separation in two patients, one with a complex of IgG and creatine kinase (EC 2.7.3.2) BB isoenzyme, the other with an IgG--alkaline phosphatase (EC 3.1.3.1) complex. Both patients had unexplainably high activities of the respective enzymes in their serum. The method we propose should be a useful, simple, routine method of detection in cases where IgG--enzyme complexes are suspected.


1986 ◽  
Vol 32 (1) ◽  
pp. 165-169
Author(s):  
G C Moses ◽  
G O Lightle ◽  
J F Tuckerman ◽  
A R Henderson

Abstract We evaluated the analytical performance of the EPOS (Eppendorf Patient Oriented System) Automated Selective Chemistry Analyzer, using the following tests for serum analytes: alanine and aspartate aminotransferases, lactate dehydrogenase, creatine kinase, gamma-glutamyltransferase, alkaline phosphatase, and glucose. Results from the EPOS correlated well with those from comparison instruments (r greater than or equal to 0.990). Precision and linearity limits were excellent for all tests; linearity of the optical and pipetting systems was satisfactory. Reagent carryover was negligible. Sample-to-sample carryover was less than 1% for all tests, but only lactate dehydrogenase was less than the manufacturer's specified 0.5%. Volumes aspirated and dispensed by the sample and reagent II pipetting systems differed significantly from preset values, especially at lower settings; the reagent I system was satisfactory at all volumes tested. Minimal daily maintenance and an external data-reduction system make the EPOS a practical alternative to other bench-top chemistry analyzers.


1975 ◽  
Vol 21 (1) ◽  
pp. 151-154
Author(s):  
Louis Rosenfeld

Abstract Data are presented for an electronic device that automatically halves "off-scale" signal voltages on the "SMA Flex-6" System (Technicon). This extends the usefulness of the system by obviating the need for most repeat analyses on dilutions of specimens containing constituents in concentrations that exceed the limits of the pre-calibrated chart paper. Accurate results are obtained because the chemical reactions are shown to be linear up to nearly twice the maximum calibration on the recorder paper for the following analytes: bilirubin, total and direct (20.0 mg/dl); alkaline phosphatase (700 U/ liter); lactate dehydrogenase (1200 U/liter); creatine kinase (2400 U/liter); and aspartate aminotransferase (600 U/liter). In contrast, dilution of sera 2-, 5-, and 10-fold with sodium chloride solution (8.5 g/liter) produces positive errors ranging from 6 to 38% for these enzymes, but has no significant effect on bilirubin.


Author(s):  
R T P Jansen ◽  
A P Jansen

In a trial of the Netherlands coupled external/internal quality control program a control serum and an enzyme standard were analysed over a period of eight weeks, five times each week. Five enzymes were determined: alkaline phosphatase, creatine kinase, lactate dehydrogenase, alanine aminotransferase, and γ-glutamyltransferase. The measured values in the serum were converted to the standards. Those laboratories using the recommended methods also submitted their non-transformed serum values. The following standardisation techniques have been compared: ( a) no standardisation of methodology but use of enzyme standards; ( b) standardisation of methodology; ( c) standardisation of methodology combined with use of an enzyme standard. Results were submitted to analysis of variance. Standardisation of methodology did not yield smaller interlaboratory variation than the standardisation with enzyme standards. In this trial a combination of both standardisation techniques yielded generally better results. Results for γ-glutamyltransferase indicate that standardisation of substrate may be necessary apart from the use of an enzyme standard. The preparation of stable enzyme standards is stressed.


Author(s):  
Alexandra K. Mason ◽  
Sean M. Perry ◽  
Mark A. Mitchell

Abstract OBJECTIVE To measure plasma and tissue activities of alkaline phosphatase, alanine aminotransferase, aspartate aminotransferase (AST), creatine kinase, and γ-glutamyltransferase in 2 snake species. ANIMALS 6 banded water snakes (Nerodia fasciata) and 6 diamondback water snakes (Nerodia rhombifer). PROCEDURES Blood was collected via the ventral tail vein to measure plasma enzyme activities. Animals were then euthanized, and samples of 9 tissues were collected from each snake: skeletal muscle, cardiac muscle, liver, spleen, lung, kidney, testicle, pancreas, and gallbladder. Tissues were frozen for 30 days, then homogenized and processed. Supernatants were collected and analyzed within 24 hours of processing. A linear mixed model was used to determine differences in enzyme activity between tissues and species and assess interactions between tissues and species. RESULTS Activities of all enzymes were found to differ significantly among tissues. There were also significant differences between species for all enzyme activities, except AST activity. The kidney had the highest alanine aminotransferase and γ-glutamyltransferase activities. Alkaline phosphatase activity was significantly highest in liver and kidney tissues than in other tissue. Creatine kinase activity was highest in skeletal muscle, followed by cardiac muscle and kidney. AST activity was present in all tissues evaluated, but was highest in liver, kidney, and cardiac muscle in both species. CLINICAL RELEVANCE Results reinforced the importance of characterizing the origin of tissue enzymes in reptiles to improve our understanding of biochemistry results and highlighted the differences that can exist in tissue enzyme activities between closely related species.


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