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At least 199 records · Page 11Linked to original sources
PubMed1990

Nutritive value of rubber seed (Hevea brasiliensis) meal: utilization by growing pigs of semipurified diets in which rubber seed meal partially replaced soybean meal.

Thirty-six four-way cross (Chester White X Landrace X Large White X Yorkshire) growing barrows and gilts were used to investigate the effects of replacing graded levels of protein from soybean meal with equivalent levels of protein from rubber seed meal in 16% CP semipurified diets on the performance characteristics, hematocrit, plasma metabolites and N utilization of pigs. The first diet (control) was largely cornstarch-soybean meal in which the soybean meal supplied all of the CP. In other diets, rubber seed meal replaced 10%, 20% and 30%, respectively, of the protein of soybean meal in the control diet. Twenty gilts were used in a 28-d growth trial and 16 barrows were used in an 8-d digestion trial (4-d collection). There were no differences (P greater than .05) in ADG, ADF intake and in the feed:gain ratios, even though there was a trend for lower ADG and gain:feed ratio as the level of rubber seed meal increased in the diet. There were no differences in hematocrit, but plasma protein and albumin tended to be depressed when rubber seed meal provided more than 10% of the dietary protein. Apparent digestibilities of GE, DM and N were lower with rubber seed meal at 20% of the protein than with any other diet, but apparent N retained and the percent of digested N retained were not depressed significantly (P greater than .05). Although rubber seed meal protein is of poorer quality than soybean meal protein for growing pigs, at least 10% of dietary protein can be provided by rubber seed meal without adversely affecting growth and N utilization.

Animal Feed↗
PubMed1991

Co- and post-translational processing of the hevein preproprotein of latex of the rubber tree (Hevea brasiliensis)

Hevein is a chitin-binding protein of 43 amino acids found in the lutoid body-enriched fraction of rubber tree latex. A hevein cDNA clone (HEV1) (Broekaert, W., Lee, H.-i., Kush, A., Nam, C.-H., and Raikhel, N. (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 7633-7637) encodes a putative signal sequence of 17 amino acids followed by a polypeptide of 187 amino acids. Interestingly, this polypeptide has two distinct domains: an amino-terminal domain of 43 amino acids, corresponding to mature hevein, and a carboxyl-terminal domain of 144 amino acids. To investigate the mechanisms involved in processing of the protein encoded by HEV1, three domain-specific antisera were raised against fusion proteins harboring the amino-terminal domain (N domain), carboxyl-terminal domain (C domain), and both domains (NC domain). Translocation experiments using an in vitro translation system show that the first 17-amino acid sequence encoded by the cDNA functions as a signal peptide. Immunoblot analysis of proteins extracted from lutoid bodies demonstrates that a 5-kDa protein comigrated with purified mature hevein and cross-reacted with N domain- and NC domain-specific antibodies. A 14-kDa protein was recognized by C domain- and NC domain-specific antibodies. A 20-kDa protein was cross-reactive with all three antibodies. Microsequencing data further suggest that the 5-kDa (amino-terminal domain) and 14-kDa (carboxyl-terminal domain) proteins are post-translational cleavage products of the 20-kDa polypeptide (both domains) which corresponds to the proprotein encoded by HEV1. In addition, it was found that the amino-terminal domain could provide chitin-binding properties to a fusion protein bearing it either amino terminally or carboxyl terminally.

Antimicrobial Cationic Peptides↗