Activation energy and lectin affinity chromatography of gamma-glutamyltransferase as a marker for enzyme heterogeneity

Delanghe, Joris; Buyzere, Marc L. De; Scheerder, Ivan K. De; Faust, U.; Wieme, R.J.

doi:10.1016/s0009-9120(89)80008-6

Cited by 10 publications

(4 citation statements)

References 21 publications

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“…Delanghe et al (l l, 12) have shown that in all types of liver diseases except extrahepatic obstruction, the activation energy of serum -glutamyltransferase is signiflcantly higher than in the reference population, and that the differences are proportional to the amount of sialic acid attached to the molecule. The lowering of the activation energy obtained after neuraminidase treatment suggests that the presence of sialic acid can be regarded äs a steric hindrance for the active site of the -glutamyltransferase (11).…”

Section: Discussionmentioning

confidence: 99%

“…Delanghe et al have shown that both affmity chromatography behaviour (12) and activation energy (11,12) are independent of total serum -glutamyltransferase activity. Similarly, we have not found a significant correlation between the total serum S'-nucleotidase activity and activation energy.…”

Section: Discussionmentioning

confidence: 99%

“…A greater sialylation could lead to a decrease in its clearance rates. Delanghe et al (l J,12) found that, in patients with liver diseases, the activation energy pf seruin Y^glutamyltransferase (EC 2.3.2.2) is higher than in normal individuals, and related to a greater amount of sialic acid attached to the molecule. Delanghe et al (l J,12) found that, in patients with liver diseases, the activation energy pf seruin Y^glutamyltransferase (EC 2.3.2.2) is higher than in normal individuals, and related to a greater amount of sialic acid attached to the molecule.…”

Section: Introductionmentioning

confidence: 99%

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Short Communication

1994

CCLM

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Using adenosine 5'-monophosphate (Arkesteijn\ J. Clin. Chem. Clin. Biochem. 14 (1976) 155) and inosine 5'-monophosphate (Bertrand & Buret; Clin. Chim. Acta 119 (1982) 275) äs Substrates for the determination of serum 5 f -nucleotidase, linear Arrhenius plots were obtained between 25 °C and 37 °C. With the latter method, in patients with hepatobiliary disease, activation energy is higher than in healthy subjects (67.8 ± 0.8 kJ · mol" 1 vs. 59.2 ± 1.6 kJ -mol" 1 , p < 0.001). Neuraminidase treatment resulted in a significant reduction in the activation energy of serum 5'-nucleotidase from patients (63.6 ± 0.6 kJ · mol" 1 , p < 0.001). Although the activation energy seen is also influenced by conditions other than sialic acid content, the results obtained are in accordance with the hypothesis that in liver disease serum 5-nucleotidase becomes more sialylated.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Short Communication

1994

CCLM

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“…There are some reports describing the use of different lectins for evaluation of cell surfaces [172,173], for blood typing [174,175], as mitogenic agents [176,177,178,179,180], to detect changes in cellular transformation [181,182], in the clearance of sulfated glycoprotein hormones, control of glycoprotein biosynthesis, cell-cell interactions in the immune system [183] and associated with susceptibility and severity in a wide variety of infectious and autoimmune diseases [184,185]. Moreover, lectins can also be applied in laboratory and chemical analyses [173,178,186], since they are easily immobilized on inert supports [173,187].…”

Section: Biotechnological Potentialmentioning

confidence: 99%

Insights into Animal and Plant Lectins with Antimicrobial Activities

et al. 2015

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Abstract:Lectins are multivalent proteins with the ability to recognize and bind diverse carbohydrate structures. The glyco -binding and diverse molecular structures observed in these protein classes make them a large and heterogeneous group with a wide range of biological activities in microorganisms, animals and plants. Lectins from plants and animals are commonly used in direct defense against pathogens and in immune regulation. This review focuses on sources of animal and plant lectins, describing their functional classification and tridimensional structures, relating these properties with biotechnological purposes, including antimicrobial activities. In summary, this work focuses on structural-functional elucidation of diverse lectin groups, shedding some light on host-pathogen interactions; it also examines their emergence as biotechnological tools through gene manipulation and development of new drugs.

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