4. What glycoprotein is present in saliva? What it its function?

The protective functions of saliva are attributed, in part, to its serous and mucous glycoproteins.
We have studied, as representative molecules, the proline-rich glycoprotein (PRG) from human
parotid saliva and the high (MG1) and low (MG2) molecular weight mucins from submandibularsublingual saliva. PRG (38.9 kDa) contains 40% carbohydrate consisting of 6 triantennary Nlinked units and a single peptide chain of 231 amino acids, 75% of which = PRO + GLY + GLN.
PRG's secondary structure is comprised of 70% random coil (naked regions) and 30% beta-turns
(glycosylated domains). MG1 (greater than 10(3) kDa) contains 15% protein (several disulfide
linked subunits), 78% carbohydrate (290 units of 4-16 residues), 7% sulfate, and small amounts
of covalently linked fatty acids. MG2 (200-250 kDa) contains 30% protein (single peptide chain),
68% carbohydrate (170 units of 2-7 residues), and 2% sulfate. The major carbohydrate units of
MG2 are: NeuAc alpha 2,3Gal beta 1,3GalNAc,Gal beta 1,3GalNAc, and Fuc alpha 1,2Gal beta
1,3GalNAc. MG1 contains hydrophobic domains, as evidenced by its ability to bind fluorescent
hydrophobic probes; MG2 does not. Collectively, the biochemical and biophysical comparisons
between MG1 and MG2 indicate that these two mucins are structurally different. Several
functional properties of MG1, MG2, and PRG have been examined, including their presence in
two-hour in vivo enamel pellicle, binding to synthetic hydroxyapatite, lubricating properties, and
interactions with oral streptococci. The data presented suggest that these glycoproteins may
have multiple functions which are predicated, in part on their carbohydrate units. The potential
significance of the structure-function relationships of these glycoproteins to the oral ecology is
discussed.
http://www.ncbi.nlm.nih.gov/pubmed/3305626
The high-molecular-mass salivary mucin MG1, one of two major mucins produced by human
salivary glands, plays an important role in oral health by coating the tooth surface and by acting
as a bacterial receptor. Here this mucin was purified from the submandibular/sublingual saliva of
a blood group O individual. The presence of MUC5B as the major mucin in this preparation was
confirmed by amino acid analysis and its reactivity with the monoclonal antibody PAN H2. To
structurally characterize MG1 carbohydrates the O-glycans were released by reductive elimination. Nuclear magnetic resonance spectroscopy of the nonfractionated mixture showed
that (1) fucose was present in blood group H, Le a, Lex, Leb, and Ley epitopes; (2) NeuAc was
mainly linked 2-3 to Gal or 2-6 to GalNAcol; and (3) the major internal structures were core 1
and core 2 sequences. After this preliminary analysis the released oligosaccharides were
separated into neutral (56%), sialylated (26%), and sulfated (19%) fractions, with an average
length of 13, 17, and 41 sugar residues, respectively. Gas chromatographymass spectrometry
and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry of mixtures of
neutral and sialylated oligosaccharides revealed at least 62 neutral and 25 sialylated
oligosaccharides consisting of up to 20 monosaccharide residues. These results showed that the
MG1-derived oligosaccharides were much longer than those of MG2, and only a few species were
found on both molecules. Thus, these two mucins create an enormous repertoire of potential
binding sites for microorganisms at one of the major portals where infectious organisms enter
the body.
http://glycob.oxfordjournals.org/content/12/1/1.full
The protective functions of saliva are attributed, in part, to its serous and mucous glycoproteins.
We have studied, as representative molecules, the proline-rich glycoprotein (PRG) from human
parotid saliva and the high (MG1) and low (MG2) molecular weight mucins from submandibular-

sublingual saliva. PRG (38.9 kDa) contains 40% carbohydrate consisting of 6 triantennary Nlinked units and a single peptide chain of 231 amino acids, 75% of which = PRO + GLY + GLN.
PRG's secondary structure is comprised of 70% random coil (naked regions) and 30% beta-turns
(glycosylated domains). MG1 (greater than 10(3) kDa) contains 15% protein (several disulfide
linked subunits), 78% carbohydrate (290)
http://www.ncbi.nlm.nih.gov/pubmed/3305626

What is ptyalin made up of?

- A form of amylase in the saliva of humans and some animals that catalyzes the hydrolysis of starch
into maltose and dextrin. Ptyalin is a mixture of two enzymes- alpha-amylase and beta-amylase.
Ptyalin acts on linear (1,4) glycosidic linkages, but compound hydrolysis requires an enzyme that
acts on branched products.

http://www.answers.com/topic/ptyalin

Amylase is found in saliva and breaks starch into maltose and dextrin. This form of amylase is also called "ptyalin" /
taln/[4] It will break large, insoluble starch molecules into soluble starches (amylodextrin, erythrodextrin,
and achrodextrin) producing successively smaller starches and ultimately maltose. Ptyalin acts on linear
(1,4) glycosidic linkages, but compound hydrolysis requires an enzyme that acts on branched products. Salivary
amylase is inactivated in the stomach by gastric acid. In gastric juice adjusted to pH 3.3, ptyalin was totally
inactivated in 20 minutes at 37C. In contrast, 50% of amylase activity remained after 150 minutes of exposure to
gastric juice at pH 4.3.[5] Both starch, the substrate for ptyalin, and the product (short chains of glucose) are able to
partially protect it against inactivation by gastric acid. Ptyalin added to buffer at pH 3.0 underwent complete
inactivation in 120 minutes; however, addition of starch at a 0.1% level resulted in 10% of the activity remaining, and
similar addition of starch to a 1.0% level resulted in about 40% of the activity remaining at 120 minutes. [6]

http://en.wikipedia.org/wiki/Alpha-amylase

Salivary Amylase (ptyalin) - made in the salivary glands, functions in mouth to hydrolyze (break down) starch to
maltose (disaccharide)
http://www.biology-online.org/biology-forum/about1602Salivary%20Amylase%20(ptyalin)%20-%20made%20in%20the
%20salivary%20glands,%20functions%20in%20mouth%20to%20hydrolyze%20(break%20down)%20starch%20to%20maltose
%20(disaccharide)9.html?p=111023&hilit=Ptyalin#p111023