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Trypsin digest mass spectrometry analysis of the protein cocktail and purified Tf. Both figures show the ten most abundant proteins and cover > 99% of all proteins in the sample. (A) Represents the protein composition of the protein cocktail that was used as the starting material for the purification of Tf. The error bars were derived from three separate purifications. (B) Represents the protein composition of the purified Tf. The error bars were derived from three separate purifications. Abbreviations: ALB, albumin; APOA1, apolipoprotein A‐I; APOA2, apolipoprotein A‐II; APOH, beta‐2‐glycoprotein; CFI, complement factor I; CP, ceruloplasmin; GC, vitamin D‐binding protein; HBA1, <t>hemoglobin</t> subunit alpha; HBB, hemoglobin subunit beta; HP, haptoglobin; HPR, haptoglobin related protein; HPX, hemopexin; IGG1, immunoglobulin gamma‐1 heavy chain; IGHG4, immunoglobulin heavy constant gamma 4; RBP4, retinol‐binding protein 4; SERPINA1, alpha‐1‐antitrypsin; TF, transferrin.
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Trypsin digest mass spectrometry analysis of the protein cocktail and purified Tf. Both figures show the ten most abundant proteins and cover > 99% of all proteins in the sample. (A) Represents the protein composition of the protein cocktail that was used as the starting material for the purification of Tf. The error bars were derived from three separate purifications. (B) Represents the protein composition of the purified Tf. The error bars were derived from three separate purifications. Abbreviations: ALB, albumin; APOA1, apolipoprotein A‐I; APOA2, apolipoprotein A‐II; APOH, beta‐2‐glycoprotein; CFI, complement factor I; CP, ceruloplasmin; GC, vitamin D‐binding protein; HBA1, <t>hemoglobin</t> subunit alpha; HBB, hemoglobin subunit beta; HP, haptoglobin; HPR, haptoglobin related protein; HPX, hemopexin; IGG1, immunoglobulin gamma‐1 heavy chain; IGHG4, immunoglobulin heavy constant gamma 4; RBP4, retinol‐binding protein 4; SERPINA1, alpha‐1‐antitrypsin; TF, transferrin.
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Trypsin digest mass spectrometry analysis of the protein cocktail and purified Tf. Both figures show the ten most abundant proteins and cover > 99% of all proteins in the sample. (A) Represents the protein composition of the protein cocktail that was used as the starting material for the purification of Tf. The error bars were derived from three separate purifications. (B) Represents the protein composition of the purified Tf. The error bars were derived from three separate purifications. Abbreviations: ALB, albumin; APOA1, apolipoprotein A‐I; APOA2, apolipoprotein A‐II; APOH, beta‐2‐glycoprotein; CFI, complement factor I; CP, ceruloplasmin; GC, vitamin D‐binding protein; HBA1, <t>hemoglobin</t> subunit alpha; HBB, hemoglobin subunit beta; HP, haptoglobin; HPR, haptoglobin related protein; HPX, hemopexin; IGG1, immunoglobulin gamma‐1 heavy chain; IGHG4, immunoglobulin heavy constant gamma 4; RBP4, retinol‐binding protein 4; SERPINA1, alpha‐1‐antitrypsin; TF, transferrin.
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Trypsin digest mass spectrometry analysis of the protein cocktail and purified Tf. Both figures show the ten most abundant proteins and cover > 99% of all proteins in the sample. (A) Represents the protein composition of the protein cocktail that was used as the starting material for the purification of Tf. The error bars were derived from three separate purifications. (B) Represents the protein composition of the purified Tf. The error bars were derived from three separate purifications. Abbreviations: ALB, albumin; APOA1, apolipoprotein A‐I; APOA2, apolipoprotein A‐II; APOH, beta‐2‐glycoprotein; CFI, complement factor I; CP, ceruloplasmin; GC, vitamin D‐binding protein; HBA1, <t>hemoglobin</t> subunit alpha; HBB, hemoglobin subunit beta; HP, haptoglobin; HPR, haptoglobin related protein; HPX, hemopexin; IGG1, immunoglobulin gamma‐1 heavy chain; IGHG4, immunoglobulin heavy constant gamma 4; RBP4, retinol‐binding protein 4; SERPINA1, alpha‐1‐antitrypsin; TF, transferrin.
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Trypsin digest mass spectrometry analysis of the protein cocktail and purified Tf. Both figures show the ten most abundant proteins and cover > 99% of all proteins in the sample. (A) Represents the protein composition of the protein cocktail that was used as the starting material for the purification of Tf. The error bars were derived from three separate purifications. (B) Represents the protein composition of the purified Tf. The error bars were derived from three separate purifications. Abbreviations: ALB, albumin; APOA1, apolipoprotein A‐I; APOA2, apolipoprotein A‐II; APOH, beta‐2‐glycoprotein; CFI, complement factor I; CP, ceruloplasmin; GC, vitamin D‐binding protein; HBA1, hemoglobin subunit alpha; HBB, hemoglobin subunit beta; HP, haptoglobin; HPR, haptoglobin related protein; HPX, hemopexin; IGG1, immunoglobulin gamma‐1 heavy chain; IGHG4, immunoglobulin heavy constant gamma 4; RBP4, retinol‐binding protein 4; SERPINA1, alpha‐1‐antitrypsin; TF, transferrin.

Journal: Biotechnology and Bioengineering

Article Title: Transferrin Purification, Biophysical Characterization, and Lung Biodistribution in Sickle Cell Disease Mice

doi: 10.1002/bit.70012

Figure Lengend Snippet: Trypsin digest mass spectrometry analysis of the protein cocktail and purified Tf. Both figures show the ten most abundant proteins and cover > 99% of all proteins in the sample. (A) Represents the protein composition of the protein cocktail that was used as the starting material for the purification of Tf. The error bars were derived from three separate purifications. (B) Represents the protein composition of the purified Tf. The error bars were derived from three separate purifications. Abbreviations: ALB, albumin; APOA1, apolipoprotein A‐I; APOA2, apolipoprotein A‐II; APOH, beta‐2‐glycoprotein; CFI, complement factor I; CP, ceruloplasmin; GC, vitamin D‐binding protein; HBA1, hemoglobin subunit alpha; HBB, hemoglobin subunit beta; HP, haptoglobin; HPR, haptoglobin related protein; HPX, hemopexin; IGG1, immunoglobulin gamma‐1 heavy chain; IGHG4, immunoglobulin heavy constant gamma 4; RBP4, retinol‐binding protein 4; SERPINA1, alpha‐1‐antitrypsin; TF, transferrin.

Article Snippet: Auto‐oxidation of human hemoglobin (Hb) was monitored on a Hewlett‐Packard 8452A spectrophotometer (HP, Palo Alto, CA).

Techniques: Mass Spectrometry, Purification, Derivative Assay, Binding Assay