Id |
Subject |
Object |
Predicate |
Lexical cue |
T32 |
0-188 |
Sentence |
denotes |
Human LF is a cationic glycosylated protein consisting of 691 amino acids (9) folded into two globular lobes (80 kDa bi-lobal glycoprotein) (10), that are connected by an α-helix (11, 12). |
T33 |
189-229 |
Sentence |
denotes |
Bovine LF contains 689 amino acids (13). |
T34 |
230-403 |
Sentence |
denotes |
LF was first discovered and isolated from bovine milk in 1939 (14), and is a member of the transferrin family (60% amino acid sequence identity with serum transferrin) (11). |
T35 |
404-628 |
Sentence |
denotes |
LF and transferrin have similar amino acid compositions, secondary structures (including their disulphide linkages), and tertiary structures, although they differ in terms of biological functions (11, 15, 16) (see Figure 2). |
T36 |
629-787 |
Sentence |
denotes |
There are also three different isoforms: LF-α is the iron-binding isoform, while LF- β and LF-g both have ribonuclease activity but do not bind iron (11, 17). |
T37 |
788-882 |
Sentence |
denotes |
When it is iron-rich it is referred to hololactoferrin and when iron-free apolactoferrin (18). |
T38 |
883-1120 |
Sentence |
denotes |
The tertiary structures of the two forms are significantly different: apolactoferrin is characterized by an open conformation of the N-lobe and a closed conformation of the C-lobe, while both lobes are closed in the hololactoferrin (18). |
T39 |
1121-1309 |
Sentence |
denotes |
Human LF and bovine LF possess high sequence homology and have very similar antibacterial, antifungal, antiviral, antiparasitic, anti-inflammatory, and immunomodulatory activities (19–21). |
T40 |
1310-1418 |
Sentence |
denotes |
Consequently, it is common to give the bovine form rather than say a recombinant human form as a supplement. |
T41 |
1419-1590 |
Sentence |
denotes |
Bovine LF is also deemed a “generally recognized as safe” substance by the Food and Drug Administration (FDA, USA), and is commercially available in large quantities (19). |