“Haemagglutinins” of the Phaeophyceae and Non-specific Aggregation Phenomena by Polyphenols

Rogers, David J.; Loveless, R. W.

doi:10.1515/botm.1985.28.4.133

Cited by 11 publications

(6 citation statements)

References 15 publications

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“…Rogers and Loveless (1985) and Blunden et al (1986) have shown that extracts of brown algae, including that of A. nodosum, no longer 'agglutinate' erythrocytes if polyphenols are removed from the extracts with insoluble PVPP. Fabregas et al (1986) have made similar observations.…”

Section: Resultsmentioning

confidence: 99%

“…However, this work by Rogers and Loveless (1985) did not entirely resolve the situation as the possibility remained that true lectins had been removed from the brown algal extracts along with the polyphenols, due to non-specific binding of the lectins by the polyphenols.…”

Section: Introductionmentioning

confidence: 94%

“…Doubt exists, therefore, if the reported haemagglutinating activity in extracts of brown algae is actually due to true lectins. Rogers & Loveless (1985) investigated this problem and showed that polyphenol-free extracts of six brown algae lacked haemagglutinating activity, although 'haemagglutination' was produced by polyphenolcontaining crude extracts of the six algae and by purified polyphenols from these six species. It was suggested that the previously reported agglutination of human erythrocytes by extracts of brown algae was due to the presence of polyphenols in these extracts rather than the presence of true lectins.…”

Section: Introductionmentioning

confidence: 99%

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Electron microscopy of human erythrocytes agglutinated by lectin from Codium fragile ssp. tomentosoides and pseudo-haemagglutinin from Ascophyllum nodosum

Rogers

Loveless

1991

J Appl Phycol

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Human erythrocytes were exposed to extracts of Codiumfragile ssp. tomentosoides, Ascophyllum nodosum, Dolichos biflorus seeds and a solution of purified polyphenols from Ascophyllum nodosum. In each case the erythrocytes appeared to agglutinate. Agglutinates were examined by scanning electron microscopy. Photomicrographs of the erythrocytes exposed to lectin-containing extracts of C. fragile and D. biflorus showed the typical appearance of agglutinated cells. Photomicrographs of the erythrocytes exposed to the crude extract and purified polyphenols from A. nodosum were similar to each other, but quite different in appearance to erythrocytes agglutinated by the lectins from C. fragile and D. biflorus. This evidence adds further support to the contention that lectin presence recorded in brown algal extracts is largely due to 'pseudoagglutination' produced by polyphenols contained in these extracts.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 94%

Section: Introductionmentioning

confidence: 99%

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Electron microscopy of human erythrocytes agglutinated by lectin from Codium fragile ssp. tomentosoides and pseudo-haemagglutinin from Ascophyllum nodosum

Rogers

Loveless

1991

J Appl Phycol

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“…Indeed, the polyphenols may be expected to inhibit most enzymes and react with most other proteins (Loomis, 1974). The non-dialysable polyphenols from A. nodosum and some other brown algae have been shown to cause nonspecific aggregation of human erythrocytes (Rogers & Loveless, 1985;Blunden et al, 1986), presumably because one polyphenol molecule can react with protein at the cell surface of several erythrocytes.…”

Section: Discussionmentioning

confidence: 99%

Isolation and characterization of brown algal polyphenols as inhibitors of α-amylase, lipase and trypsin

1989

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Extracts of Ascophyllum nodosum, Fucus serratus, F. vesiculosus and Pelvetia canaliculata contain inhibitorsof a-amylase, lipase and trypsin. The inhibitors were isolated and identified by 'H NMR spectroscopy as polyphenols which have apparent molecular weights in the range from 30000 to 100 000 daltons, as determined by ultra-filtration with Amicon membranes. These polyphenols account for the whole of the inhibitory activity in crude algal extracts. The compounds inhibit a-amylase and trypsin in an apparently non-competitive manner, when preincubated with the enzymes, and the inhibition is directly proportional to the concentration of the inhibitor. Starch protects a-amylase when added to the enzyme together with the inhibitors. Under this condition the effectiveness of the inhibitors is reduced ten-fold.

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“…Apparently, HA was more due to the polyphenols content of the P. minor that was co-extracted with the lectins than the P. minor lectin. According to Rogers and Loveless (1985), polyphenols were reported to have strong HA. However, lectin HA is based on the specific interaction of lectin with the erythrocytes' The false hemagglutinating capacity of polyphenols might become a concern for research on lectin of brown algae (Cortés-giraldo et al, 2012) which resulted in the small number of the Phaeophyta lectin researches.…”

Section: Resultsmentioning

confidence: 99%

Extraction and Partial Characterization of Lectin from Indonesian Brown Algae Padina australis and Padina minor

Fajarningsih

Intaqta

Praseptiangga

et al. 2019

Squalen Bull. Marine Fisheries Postharvest Biotech.

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Extraction and partial characterization of lectin from Indonesian Padina australis and Padina minor had been carried out. The crude extract of the P. australis and P. minor were examined for hemagglutination activity (HA) using native and trypsin-treated of rabbit and human A, B, O type erythrocytes. Both extracts agglutinated all of the trypsintreated erythrocytes tested in the HA assay. Strong HA was detected in the crude extract of P. minor with trypsintreated of human type A and O erythrocytes. However, the sugar-binding specificity study through the quantitative hemagglutination inhibition (HI) assay showed that P. minor extract could not specifically recognize the glycans tested. Apparently, the HA of the P. minor was more due to its co-extracted polyphenols content than its lectin content. On the other hand, the HI assay showed that asialo transferrin human (aTf) and asialo porcine thyroglobulin (aPTG) were the most powerful in inhibiting the HA of P. australis. Those indicated that P. australis protein extract was able to specifically recognized aTf and aPTG. The stability of P. australis and P. minor HA over various temperatures, pH ranges, and divalent cations studies showed that the P. minor HA was stable on a wide range of pH and temperature; not affected by the presence of EDTA, but decreased by Ca 2+ and Mg 2+ additions showed that P. minor protein extract was not a metallic protein. The HA of P. australis decreased at 60 o C and was inactivated at 90 o C; increased at strong acidic (pH 3 & 4) and strong basic (pH 9 & 10) and dependent by the presence of either EDTA or Ca 2+ and Mg 2+ divalent cation.

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“Haemagglutinins” of the Phaeophyceae and Non-specific Aggregation Phenomena by Polyphenols

Cited by 11 publications

References 15 publications

Electron microscopy of human erythrocytes agglutinated by lectin from Codium fragile ssp. tomentosoides and pseudo-haemagglutinin from Ascophyllum nodosum

Electron microscopy of human erythrocytes agglutinated by lectin from Codium fragile ssp. tomentosoides and pseudo-haemagglutinin from Ascophyllum nodosum

Isolation and characterization of brown algal polyphenols as inhibitors of α-amylase, lipase and trypsin

Extraction and Partial Characterization of Lectin from Indonesian Brown Algae Padina australis and Padina minor

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