Storage Proteins from Lathyrus sativus Seeds

Abstract

The proteins from Lathyrus sativus Linn. (chickling vetch or grass pea) seeds were investigated. Protein constitutes approximately 20% of the seed dry weight, >60% of which is composed by globulins and 30% by albumins. A single, 24 kDa polypeptide comprises more than half of the protein present in the albumin fraction. The globulins may be fractionated into three main components, which were named alpha-lathyrin (the major globulin), beta-lathyrin, and gamma-lathyrin. alpha-Lathyrin, with a sedimentation coefficient of approximately 18S, is composed of three main types of unglycosylated subunits (50-66 kDa), each of which produce, upon reduction, a heavy and a light polypeptide chain, by analogy with 11S. beta-Lathyrin, with a sedimentation coefficient of 13S, is composed by a relatively large number of subunits (8-66 kDa). Two major polypeptides are glycosylated and exhibit structural similarity with beta-conglutin from Lupinus albus. One of these possesses an internal disulfide bond. gamma-Lathyrin, with a sedimentation coefficient of approximately 5S, contains two interacting, unglycosylated polypeptides, with no disulfide bonds: the major 24 kDa albumin and the heavier (20 kDa) polypeptide chain of La. sativus lectin.

Evaluation of Turkish grass pea (Lathyrus sativus L.) collections for it agronomic characters with a special reference to ODAP content

“…It is observed that genotypes affected by year at different levels in terms of protein when examined separately and, the highest protein content was determined in landrace 2002 (30.10%) in 2013 and in landrace 6416 (31.52%) in 2014 ( Figure 2). Protein content of grass pea could reach up to 34% (Rosa et al, 2000). Grella et al (2010) investigated thirty-one European accessions of grass pea and reported that protein ratio varied between 22.87 and 31.29%.…”

Characterization of Italian grasspea (Lathyrus sativus L.) germplasm using agronomic traits, biochemical and molecular markers

“…Globulins comprise three main components: a-lathyrin, b-lathyrin and c-lathyrin (Rosa et al 2000). a-lathyrin represents about 80% of the globulin fraction and consists of 11S legumin polypeptides made up of disulfide linked subunits.…”

Crystal Structure and Functional Insights of Hemopexin Fold Protein from Grass Pea

“…Although proteins constitute approximately 20% of the total seed dry weight (Rosa et al, 2000), the grass pea crop has presently been banned due to the presence of various antinutritional substances responsible for neurolathyrism (Grela et al, 2001). Also, grass pea exposure results in occupational allergies leading to asthma and rhinoconjunctivitis in susceptible individuals (Valdivieso et al, 1988;Porcel et al, 2001;Gironés et al, 2005).…”