Gene/Protein
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Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
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Drug
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Target Concepts:
Gene/Protein
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Query: EC:3.5.1.52 (
PNGase F
)
1,527
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The isolation and partial characterization of
PAS-4
glycoprotein (78 kDa) from bovine milk fat globule membrane (MFGM) is described.
PAS-4
was selectively extracted with Triton X-114 nonionic detergent and then fractionated on DEAE-Sepharose at pH 7.5. The
PAS-4
fraction that was not bound on DEAE-Sepharose gave a single band by SDS-PAGE. The recovery of
PAS-4
was 57.4% from MFGM. An amino acid analysis found a high percentage of nonpolar residues. Approximately 7.2% of carbohydrate from
PAS-4
was composed of mannose, galactose (Gal), N-acetylglucosamine, N-acetylgalactosamine (GalNAc), and sialic acid, most of the Gal and GalNAc in
PAS-4
being released after mild alkaline hydrolysis. This indicated that
PAS-4
contained both N- and O-linked sugar chains in concordance with the results of lectin affinity.
PAS-4
had apparent isoelectric points of 7.45, 7.41, and 7.32, but these were shifted to pI 7.47 by a neuraminidase treatment. The apparent molecular weight of
PAS-4
after deglycosylation with
N-glycanase
was approximately 57,000 by SDS-PAGE.
...
PMID:Rapid and simple procedure for purifying PAS-4 glycoprotein from bovine milk fat globule membrane. 778 99
A monoclonal antibody to the
PAS-4
glycoprotein (78 kDa) of the bovine milk fat globule membrane (MFGM) specifically recognized
PAS-4
, and was named KAS4. A component recognized by KAS4 was found in whey protein, this being a glycoprotein of 88 kDa by SDS-PAGE and named WGP-88. WGP-88 was purified and characterized in comparison with
PAS-4
. WGP-88 had apparent pI values of 6.45 and 6.39, while those of
PAS-4
were 7.39 and 7.35. Neuraminidase digestion shifted the pI values of WGP-88 to 6.57 and of
PAS-4
to 7.52. WGP-88 was rich in polar amino residues (44.9 mol%), while
PAS-4
was abundant in nonpolar amino acid residues (48.7 mol%). WGP-88 contained 17.1% of carbohydrate and
PAS-4
had 7.2%. The results of reductive hydrolysis,
N-glycanase
digestion, and a lectin blot analysis suggested that N- and O-linked sugar chains were contained in both glycoproteins. WGP-88 and
PAS-4
had a different N-terminal amino acid sequence. WGP-88 and
PAS-4
respectively inhibited competitively the binding of KAS4 to
PAS-4
and WGP-88. Our studies revealed WGP-88 recognized by KAS4 mAb to be a novel whey protein and to have different biochemical properties from those of
PAS-4
.
...
PMID:Purification and characterization of novel whey glycoprotein WGP-88 which binds to a monoclonal antibody to PAS-4 glycoprotein in the bovine milk fat globule membrane. 933 60
