scholarly journals The Amino Acid Sequence of a Protein (Apovitellenin I) From the Low-density Lipoprotein of Emu Egg Yolk

1974 ◽  
Vol 27 (1) ◽  
pp. 15 ◽  
Author(s):  
TAA Dopheide ◽  
AS Inglis
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Egg Yolk ◽  
Side Chain ◽  
Low Density ◽  
Hydrophobic Residues ◽  
Polar Residues

The amino acid sequence of apovitellenin I from emu (Dromaius novae-hollandiae) egg yolk has been determined. Difficulties were encountered during sequencing, due to a labile Tyr-Val bond, which was hydrolysed readily by trypsin, chymotrypsin and pepsin. By use of a sequenator, this bond was easily characterized. The protein contains 84 residues and is devoid of half-cystine and histidine. Hydrophobic residues occur in clusters; two very hydrophobic sequences of 12 and 13 residues are present. A very hydrophilic sequence of seven residues contains nearly one-third of all side-chain charges in the molecule; the remainder of the polar residues are scattered throughout the sequence. In a number of instances, residues with opposite charges occur in adjacent positions.

scholarly journals Amino acid sequence and domain structure of entactin. Homology with epidermal growth factor precursor and low density lipoprotein receptor.

1988 ◽  
Vol 107 (6) ◽  
pp. 2749-2756 ◽  
Author(s):  
M E Durkin ◽  
S Chakravarti ◽  
B B Bartos ◽  
S H Liu ◽  
R L Friedman ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Open Reading Frame ◽  
Low Density ◽  
Lipoprotein Receptor ◽  
Low Density Lipoprotein Receptor ◽  
Reading Frame ◽  
Density Lipoprotein Receptor

Entactin (nidogen), a 150-kD sulfated glycoprotein, is a major component of basement membranes and forms a highly stable noncovalent complex with laminin. The complete amino acid sequence of mouse entactin has been derived from sequencing of cDNA clones. The 5.9-kb cDNA contains a 3,735-bp open reading frame followed by a 3'-untranslated region of 2.2 kb. The open reading frame encodes a 1,245-residue polypeptide with an unglycosylated Mr of 136,500, a 28-residue signal peptide, two Asn-linked glycosylation sites, and two potential Ca2+-binding sites. Analysis of the deduced amino acid sequence predicts that the molecule consists of two globular domains of 70 and 36 kD separated by a cysteine-rich domain of 28 kD. The COOH-terminal globular domain shows homology to the EGF precursor and the low density lipoprotein receptor. Entactin contains six EGF-type cysteine-rich repeat units and one copy of a cysteine-repeat motif found in thyroglobulin. The Arg-Gly-Asp cell recognition sequence is present in one of the EGF-type repeats, and a synthetic peptide from the putative cell-binding site of entactin was found to promote the attachment of mouse mammary tumor cells.

Characterization of glycopeptides derived from the low-density lipoprotein of hen's egg yolk

1968 ◽  
Vol 46 (8) ◽  
pp. 983-988 ◽  
Author(s):  
J. Z. Augustyniak ◽  
W. G. Martin
Keyword(s):  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Egg Yolk ◽  
Low Density ◽  
Amide Nitrogen ◽  
Acetylneuraminic Acid ◽  
Hen’S Egg ◽  
Terminal Amino ◽  
Protein Moiety

Two glycopeptides (A and B) were isolated from pronase-digested vitellenin, the protein moiety of the low-density lipoprotein of hen's egg yolk. Aspartic acid was the only N-terminal amino acid of both glycopeptides but only A contained N-acetylneuraminic acid. A contained 55% hexose (mannose), 14% hexosamine, 12% N-acetylneuraminic acid, 0.71% amide nitrogen, and its molecular weight was 2.3 × 103. The corresponding values for B were 64, 17, 0.0, 0.75, and 2.0 × 103. Chemical analyses showed that B (and probably A) occurs in vitellenin with the heteropolysaccharide group bound N-glycosidically via the β-amide group of an asparaginyl residue. The indicated structure is R∙(NH)Asp∙Thr∙Ser∙(Ala, Gly, Val)∙Ile, where R, the heteropolysaccharide group, contains 2 hexosamine and 8 hexose residues.

scholarly journals Highly efficient extraction and purification of low-density lipoprotein from hen egg yolk

2018 ◽  
Vol 97 (6) ◽  
pp. 2230-2238 ◽  
Author(s):  
N. Wang ◽  
Q. Xu ◽  
Y. Liu ◽  
Y. Jin ◽  
P.W. Harlina ◽  
...  
Keyword(s):  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Egg Yolk ◽  
Low Density ◽  
Highly Efficient ◽  
Extraction And Purification ◽  
Efficient Extraction ◽  
Hen Egg Yolk ◽  
Hen Egg
Sign in / Sign up

Export Citation Format

Share Document