Isolectins of Phaseolus vulgaris. A comprehensive study of fractionation

Pusztai, Á.; Watt, William B.

doi:10.1016/0005-2795(74)90250-5

Cited by 102 publications

(48 citation statements)

References 51 publications

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“…Pure PHA (kindly provided by Dr. A. Pusztai, The Rowett Research Institute, Scotland) used for polyclonal antibody production was isolated from red kidney beans by a procedure previously described [18]. Antiserum against PHA was produced according to the method of Harboe and Ingild [19].…”

Section: Antiseramentioning

confidence: 99%

Enteral Crude Red Kidney Bean <i>(Phaseolus vulgaris)</i> Lectin – Phytohemagglutinin – Induces Maturational Changes in the Enterocyte Membrane Proteins of Suckling Rats

Kruszewska

Kiela²,

Ljungh³

et al. 2003

Neonatology

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This study aimed to investigate the effect of enterally administered crude red kidney bean (Phaseolus vulgaris) lectin, PHA, on the expression of brush-border membrane vesicle (BBMV) proteins, in particular Na⁺/H⁺ exchangers (NHEs), in the small intestine of suckling rats. Gavage of PHA to 14-day-old rats for 3 days resulted in altered protein/glycoprotein patterns as analyzed by SDS-PAGE. Immunoblots demonstrated the appearance of two 71- and 27-kD protein bands indicative for NHE3 – one of the NHE isoforms – and PHA, respectively. PHA treatment also resulted in an augmented uptake of ²²Na⁺ by the BBMV indicating an increase in NHE activity. Overall, the data suggests that enteral PHA exposure may induce maturational changes in enterocyte membrane proteins in young rats. In view of these findings, an investigation into the addition of PHA to infant formulas and weaning diets is warranted.

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Section: Antiseramentioning

confidence: 99%

Enteral Crude Red Kidney Bean <i>(Phaseolus vulgaris)</i> Lectin – Phytohemagglutinin – Induces Maturational Changes in the Enterocyte Membrane Proteins of Suckling Rats

Kruszewska

Kiela²,

Ljungh³

et al. 2003

Neonatology

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“…Our results, however, indicated that, while the protein body fraction could not possibly have contained all the trypsin inhibitory activity, an appreciable part of it was definitely associated with it. As bean seeds contain two different families of lectins (Pusztai and Watt, 1975), their subcellular distribution could not be determined from haemagglutination tests. However, both on the basis of the highest specific activity and of the results of SDS gel electrophoresis, a major part of the lectins was found to be associated with the protein bodies.…”

Section: Discussionmentioning

confidence: 99%

COMPARTMENTALIZATION IN THE COTYLEDONARY CELLS OF PHASEOLUS VULGARIS L. SEEDS: A DIFFERENTIAL SEDIMENTATION STUDY

Pusztai¹,

Croy

Grant³

et al. 1977

New Phytologist

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SUMMARYThe appearance and the yield of sedimentable organelles from the cotyledons of Phaseolus vulgaris L. were measured with respect to the influence of the method of homogenization, the choice of dry or imbibed seeds, and the composition and the concentration of the homogenization medium. Sucrose, (0.2-0.8 M), the addition of Mg^"" (2 X 10~^M) or EDTA (3 X 10~^M) or the replacement of sucrose with mannitol made little difference to the average size distribution or the amount recovered of the 21 000 ^^v ^ 10 min pelleted organelles, the main protein body-containing fraction of the homogenate. Slicing the imbibed seeds with a razor blade or by a mechanical rotary cutter combined with a short extraction was the gentlest and the most efficient method for the production of organelles. Cell homogenates were fractionated on the basis of size by differential sedimentation into several subcellular fractions. These included a residue, starch particles (300 ^ X 10 min), a main protein body fraction (21 000 ^^v X 10 min), 38 000 ^av^ 60 min pellets, 78 000 ^av X 240 min pellets and a final supernatant. The activity in these fractions of several catabolic enzymes was measured. Most of the activity of the acidic nucleases, amylases, the BAPA-ase and a substantial part of the acidic phosphatase and the cathepsin A-type enzyme(s) were found in the supernatant, while no specific DNA-ase was found in these seeds. Protein bodies contained some of the trypsin inhibitors and most (if not all) of the lectins and Glycoprotein II. Most of the endopeptidase (azoproteinase) activity of the cotyledons appeared to be tightly bound to the cell walls or to other insoluble structural elements. Protein bodies and other intracellular organelles had very little autolytic activity and, thus, the main storage proteins of the seed were not degraded during the first 4 days of germination.

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“…In the experimental piglets oral dose of 160 HU/kg b.w. of a red kidney bean lectin preparation according to Pusztai and Watt (1974) was given. Control pigs were given 1 ml of saline to mimic the volume of the lectin administration.…”

Section: Methodsmentioning

confidence: 99%

Changes in expression of calbindin 28 kDa in the small intestine of red kidney bean (Phaseolus vulgaris) lectin-treated suckling piglets

Zacharko-Siembida¹,

Piedra²,

Arciszewski³

2013

Polish Journal of Veterinary Sciences

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Calbindin (CB) is a calcium binding protein playing a role in calcium uptake and anti-apoptotic cellular protection. The expression of CB was immunohistochemically studied in the small intestine of normal and red bean kidney lectin-treated suckling piglets. In the duodenum and jejunum (but not ileum) of lectin-treated animals overexpression of CB was noted in chromogranin A-immunoreactive (CgA-IR) neuroendocrine (NE) cells. In both control and experimental group a small population of CB-IR NE cells exhibited the presence of somatostatin (but not serotonin, histamine or CRF). After the lectin treatment, an increased (however not statistically significant) immunoreactivity to CB was found in a small subpopulation of neurons of outer submucous (but not inner submucous and myenteric) plexus. It is suggested that there is a functional interaction between lectin administration and CB-expression in the porcine small intestine. Future studies will be needed to clarify this processes.

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Isolectins of Phaseolus vulgaris. A comprehensive study of fractionation

Cited by 102 publications

References 51 publications

Enteral Crude Red Kidney Bean <i>(Phaseolus vulgaris)</i> Lectin – Phytohemagglutinin – Induces Maturational Changes in the Enterocyte Membrane Proteins of Suckling Rats

Enteral Crude Red Kidney Bean <i>(Phaseolus vulgaris)</i> Lectin – Phytohemagglutinin – Induces Maturational Changes in the Enterocyte Membrane Proteins of Suckling Rats

COMPARTMENTALIZATION IN THE COTYLEDONARY CELLS OF PHASEOLUS VULGARIS L. SEEDS: A DIFFERENTIAL SEDIMENTATION STUDY

Changes in expression of calbindin 28 kDa in the small intestine of red kidney bean (Phaseolus vulgaris) lectin-treated suckling piglets

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