Isolation and Chemical Characterization of a Mitogenic Lectin from Pisum sativum
Year: 1974
Type: article
Abstract: A mitogenic lectin has been isolated from garden peas (Pisum sativum) by affinity chromatography on Sephadex. The lectin has a molecular weight of 49,000, consists of two pairs of noncovalently linked polypeptide subunits and contains less than 0.5% by weight of carbohydrate. The small subunit (α) has a molecular weight of 7,000 and the large subunit (β) a molecular weight of 17,000. Examination of the tryptic digests of the subunits showed that the α subunit is not a fragment of the β subunit produced by a specific proteolytic cleavage. Pea lectin purified by affinity chromatography is a mixture of two closely related proteins which have the same subunit structure but which differ on a charge basis. The more acidic component (A) of pea lectin was present in about half the amount of the more basic component (B). The charge differences between the two components result exclusively from differences in their α subunits. Pea lectin has two binding sites for mannose (Ka = 1.4 x 103 liters per mole) and methyl α-d-glucoside (Ka = 0.8 x 103 liters per mole).
Source: Journal of Biological Chemistry
Author: Ian S. Trowbridge
Institution: Salk Institute for Biological Studies
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W1591050105