Studies on phytohemagglutinins XVI. Subunit structure of the pea isophytohemagglutinins

Marík, T; Entlicher, G.; Kocourek, J.

doi:10.1016/0005-2795(74)90383-3

Cited by 25 publications

(2 citation statements)

References 18 publications

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“…The amino-acid composition of affinity-purified pea root lectin did not differ from that of seed lectin, as published by Marik et al (1974) and by Hosselet et al (1983).…”

Section: -supporting

confidence: 74%

Distribution of glucose/mannose-specific isolectins in pea (Pisum sativum L.) seedlings

Diaz¹,

Hosselet

Logman

et al. 1990

Planta

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We report on the distribution and initial characterization of glucose/mannose-specific isolectins of 4- and 7-d-old pea (Pisum sativum L.) seedlings grown with or without nitrate supply. Particular attention was payed to root lectin, which probably functions as a determinant of host-plant specificity during the infection of pea roots by Rhizobium leguminosarum bv. viciae. A pair of seedling cotyledons yielded 545±49 μg of affinity-purified lectin, approx. 25% more lectin than did dry seeds. Shoots and roots of 4-d-old seedlings contained 100-fold less lectin than cotyledons, whereas only traces of lectin could be found in shoots and roots from 7-d-old seedlings. Polypeptides with a subunit structure similar to the precursor of the pea seed lectin could be demonstrated in cotyledons, shoots and roots. Chromatofocusing and isoelectric focusing showed that seed and non-seed isolectin differ in composition. An isolectin with an isoelectric point at pH 7.2 appeared to be a typical pea seed isolectin, whereas an isolectin focusing at pH 6.1 was the major non-seed lectin. The latter isolectin was also found in root cell-wall extracts, detached root hairs and root-surface washings. All non-seed isolectins were cross-reactive with rabbit antiserum raised against the seed isolectin with an isolectric point at pH 6.1. A protein similar to this acidic glucose/mannose-specific seed isolectin possibly represents the major lectin to be encountered by Rhizobium leguminosarum bv. viciae in the pea rhizosphere and at the root surface. Growth of pea seedlings in a nitrate-rich medium neither affected the distribution of isolectins nor their hemagglutination activity; however, the yield of affinity-purified root lectin was significantly reduced whereas shoot lectin yield slightly increased. Agglutination-inhibition tests demonstrated an overall similar sugar-binding specificity for pea seed and non-seed lectin. However root lectin from seedlings grown with or without nitrate supplement, and shoot lectin from nitrate-supplied seedlings showed a slightly different spectrum of sugar binding. The absorption spectra obtained by circular dichroism of seed and root lectin in the presence of a hapten also differed. These data indicate that nutritional conditions may affect the sugar-binding activity of non-seed isolectin, and that despite their similarities, seed and non-seed isolectins have different properties that may reflect tissue-specialization.

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“…The amino-acid composition of affinity-purified pea root lectin did not differ from that of seed lectin, as published by Marik et al (1974) and by Hosselet et al (1983).…”

Section: -supporting

confidence: 74%

Distribution of glucose/mannose-specific isolectins in pea (Pisum sativum L.) seedlings

Diaz¹,

Hosselet

Logman

et al. 1990

Planta

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“…Kocourek and his group (59,161) have been actively engaged in a study of the lectins of the pea Pisum sativum. They had previously reported that there Were two main peak isolectins with isolectric points of 5.9 and 7.0 and that each was com prised of two heavy (H) chains, 18,000 , and two light (L) chains, 10,500.…”

Section: Pea Lectinsmentioning

confidence: 99%

Phytohemagglutinins (Phytolectins)

Liener¹

1976

Annu. Rev. Plant. Physiol.

234

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Glucosylation of membrane-bound proteins by lipid-linked glucose

Lezica

Romero

Hopp

1978

Planta

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Particulate preparations from Pisum sativum. were able to incorporate [(14)C]glucose from UDP-[(14)C]glucose into oligosaccharide-linked lipids was formed by an oligosaccharide chain containing 7-8 glucose residues linked to dolichol, presumably via a pyrophosphate. The polymer was identified as a membrane-bound glucoprotein that could be solubilized by Triton X-100. SDS gel electrophoresis showed that a polypeptide with an apparent molecular weight of 13,000 could be glucosylated from dolichyl-phosphate-glucose. This was coincident with the electrophoretic mobility of the β subunit of the pea lectin in the same system. The glucosylated protein was solubilized from the membranes by sonication and showed the same carbohydrate-binding ability as pea lectins. These results strongly suggest that pea lectins can be glucosylated by the lipid intermediate pathway.

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Studies on phytohemagglutinins XVI. Subunit structure of the pea isophytohemagglutinins

Cited by 25 publications

References 18 publications

Distribution of glucose/mannose-specific isolectins in pea (Pisum sativum L.) seedlings

Distribution of glucose/mannose-specific isolectins in pea (Pisum sativum L.) seedlings

Phytohemagglutinins (Phytolectins)

Glucosylation of membrane-bound proteins by lipid-linked glucose

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