Variability of amino acid digestibility in different field bean cultivars for broilers

2021 ◽  
pp. 1-5
Author(s):  
J. M. Abdulla ◽  
S. P. Rose ◽  
A. M. Mackenzie ◽  
V. Pirgozliev
Keyword(s):  
1979 ◽  
Vol 23 (3) ◽  
pp. 203-210 ◽  
Author(s):  
M.N. Cenarruzabeitia ◽  
S. Santidrian ◽  
J. Bello ◽  
J. Larralde

1982 ◽  
Vol 47 (6) ◽  
pp. 1991-1994 ◽  
Author(s):  
MASAO KANAMORI ◽  
TSUNEO IKEUCHI ◽  
FUMIO IBUKI ◽  
MA KOTO KOTARU ◽  
KUANG KUNG KAN

2001 ◽  
Vol 10 (4) ◽  
pp. 309-322 ◽  
Author(s):  
K. PARTANEN ◽  
J. VALAJA ◽  
T. JALAVA

Eight white-flowered pea (Pisum sativum) and two white-flowered field bean (Vicia faba) cultivars grown organically were analysed for proximate composition and amino acid content. In vivo ileal amino acid digestibilities and faecal energy digestibility were predicted from the in vitro enzymatic digestibility of nitrogen and organic matter, respectively. The crude protein (CP) content of the pea and field bean cultivars ranged from 244 to 279 and from 320 to 347 g/kg dry matter (DM), respectively. The concentrations of several essential amino acids in protein decreased as the CP content increased. In peas, predicted in vivo digestibilities did not correlate with chemical composition, and in field beans were lower than in peas. A digestibility trial was carried out on six cannulated barrows according to a 6 ´ 5 cyclic change-over design to determine the faecal and ileal nutrient digestibilities of organically grown leafed peas (cv. Sohvi, 199 g CP/kg DM), semileafless peas (cv. Karita, 240 g CP/kg DM), field beans (cv. Kontu, 320 g CP/kg DM), narrow-leafed lupins (Lupinus angustifolius cv. Pershatsvet, 220 g CP/kg DM), and conventional warm- and cold-pressed rapeseed cakes (360 and 313 g CP/kg DM, respectively). The net energy contents of the leafed and semileafed peas, field beans, lupins, and cold- and warm-pressed rape seed cakes were 10.8, 11.2, 9.8, 9.7, 9.4 and 12.3 MJ/kg DM, respectively. The apparent ileal digestibilities of lysine and threonine were similar, but the digestibility of methionine was poor in all legume seeds. Cystine digestibility was highest in lupins and lowest in field beans. With the exception of phenylalanine, there was no difference in apparent ileal amino acid digestibilities between rapeseed cakes.;


Author(s):  
M.K. Lamvik ◽  
L.L. Klatt

Tropomyosin paracrystals have been used extensively as test specimens and magnification standards due to their clear periodic banding patterns. The paracrystal type discovered by Ohtsuki1 has been of particular interest as a test of unstained specimens because of alternating bands that differ by 50% in mass thickness. While producing specimens of this type, we came across a new paracrystal form. Since this new form displays aligned tropomyosin molecules without the overlaps that are characteristic of the Ohtsuki-type paracrystal, it presents a staining pattern that corresponds to the amino acid sequence of the molecule.


Author(s):  
A. J. Tousimis

The elemental composition of amino acids is similar to that of the major structural components of the epithelial cells of the small intestine and other tissues. Therefore, their subcellular localization and concentration measurements are not possible by x-ray microanalysis. Radioactive isotope labeling: I131-tyrosine, Se75-methionine and S35-methionine have been successfully employed in numerous absorption and transport studies. The latter two have been utilized both in vitro and vivo, with similar results in the hamster and human small intestine. Non-radioactive Selenomethionine, since its absorption/transport behavior is assumed to be the same as that of Se75- methionine and S75-methionine could serve as a compound tracer for this amino acid.


Author(s):  
Chi-Ming Wei ◽  
Margaret Hukee ◽  
Christopher G.A. McGregor ◽  
John C. Burnett

C-type natriuretic peptide (CNP) is a newly identified peptide that is structurally related to atrial (ANP) and brain natriuretic peptide (BNP). CNP exists as a 22-amino acid peptide and like ANP and BNP has a 17-amino acid ring formed by a disulfide bond. Unlike these two previously identified cardiac peptides, CNP lacks the COOH-terminal amino acid extension from the ring structure. ANP, BNP and CNP decrease cardiac preload, but unlike ANP and BNP, CNP is not natriuretic. While ANP and BNP have been localized to the heart, recent investigations have failed to detect CNP mRNA in the myocardium although small concentrations of CNP are detectable in the porcine myocardium. While originally localized to the brain, recent investigations have localized CNP to endothelial cells consistent with a paracrine role for CNP in the control of vascular tone. While CNP has been detected in cardiac tissue by radioimmunoassay, no studies have demonstrated CNP localization in normal human heart by immunoelectron microscopy.


1979 ◽  
Vol 7 (1) ◽  
pp. 261-262
Author(s):  
E. V. ROWSELL

2001 ◽  
Vol 120 (5) ◽  
pp. A153-A153
Author(s):  
S MIYAMOTO ◽  
K KATO ◽  
Y ISHII ◽  
S ASAI ◽  
T NAGAISHI ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document