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BIOSYNTHESIS OFMILK PROTEINS
By
R.KARTHIKA
Ph.D student
Department of Dairy Chemistry
WEST BENGAL UNIVERSITY OF ANIMALAND FISHERY SCIENCES
CONTENT:
NO TITLE
1 SOUCES OF AMINO ACIDS
2 SYNTHESIS OF MILK PROTEINS
3 MODIFICATIONS OF POLYPEPTIDE CHAIN
4 SECRETION OF IMMUNOGLOBULINS
5 REFERENCES
1. SOUCESOF AMINO ACIDS
1. Synthesis โ€“ Blood plasma.
Types of amino acids
Contโ€ฆ.
2. Types of EAA:
โ€ข EAA may be subdivided into those for which uptake from
blood and output in milk proteins are almost exactly
balanced (Group I).
โ€ข Those for which uptake significantly exceeds output
(Group 11).
โ€ข Group 11 amino acids are metabolized in the mammary
gland and provide amino groups, via transamination, for
the biosynthesis of those amino acids for which uptake
from blood is inadequate (Group Ill).
โ€ข Group I amino acids:
๏ƒ˜methionine,
๏ƒ˜phenylalanine,
๏ƒ˜tyrosine,
๏ƒ˜Histidine
๏ƒ˜tryptophan.
โ€ข Group II amino acids:
o valine,
o leucine,
o isoleucine,
olysine,
o Arginine
o threonine.
โ€ข Group III amino acids:
๏ฑaspartic acid,
๏ฑglutamic acid,
๏ฑglycine,
๏ฑalanine,
๏ฑserine,
๏ฑcysteine/ cystine,
๏ฑproline
2. SYNTHESIS OF MILK PROTEINS
โ€ข Synthesis of the major milk proteins occurs in the
mammary gland.
โ€ข Polymerization of the amino acids occurs on ribosomes
fixed on the rough endoplasmic reticulum of the
secretory cells, by the method common to all cells.
โ€ข The primary blueprint for the amino acid sequence of
proteins is contained in deoxyribonucleic acid (DNA)
within the cell nucleus.
CONTโ€ฆ
โ€ข The requisite information is transcribed in the nucleus to
ribonucleic acid (RNA) of which there are three types:
โ€ข messenger RNA (mRNA)
โ€ข transfer RNA (tRNA)
โ€ข ribosomal RNA (rRNA)
these are transferred to the cytoplasm where each plays a
specific role in protein synthesis.
โ€ข The specificity of the tRNAs is determined by the sequence of
the anticodon.
โ€ข Interaction between the tRNA and the appropriate amino acid
occurs in the cytoplasm but the remaining reactions in protein
synthesis occur in the ribosomes.
โ€ข The ribosomes of animal cells have a diameter of about 22 nm
and a sedimentation coefficient of 80S; they consist of two
principal subunits: 60S and 40S.
mRNA passes through a groove or tunnel between the 60S and 40S
subunits; while in the groove, mRNA is protected from the action of
ribonuclease.
โ€ข The information for the amino acid sequence is contained in the
mRNA.
โ€ข Synthesis commences at the correct codon of the mRNA because a
special amino acid derivative.
โ€ข N-formyl methionine-is bound to a specific special codon and forms
the temporary N-terminal residue of the protein.
โ€ข N-formyl methionine is later hydrolysed off, together with a short
hydrophobic signal peptide, exposing the permanent N-terminal
residue.
โ€ข The acyl amino acid-tRNA is bound to the mRNA just outside the
ribosome by becoming attached to its corresponding codon.
โ€ข Condensation is catalysed by a peptidyl transferase, which is
part of the ribosomal subunit.
โ€ข For the next cycle, a new acyl amino acid-tRNA is bound to
the mRNA, the ribosome tracks along the mRNA and the
vacated tRNA is ejected.
โ€ข Termination of synthesis is controlled by a special ribosomally-
bound protein, TB 3โ€“1, the protein release factor (RF) which
recognises any of three โ€œstop codonsโ€ UAG, UAA and UGA.
โ€ข Translocation through cell membranes is facilitated by a
signal sequence, a sequence of 15โ€“29 amino acids at the
amino terminal of the growing polypeptide chain.
โ€ข This sequence causes the ribosome to bind to the ER
membrane, in which a โ€˜channelโ€™ forms, allowing the growing
chain to enter the ER lumen.
โ€ข Subsequently, the signal sequence is cleaved from the
polypeptide by a signal peptidase, an enzyme located on the
luminal side of the ER membrane.
3. MODIFICATIONS OFTHE POLYPEPTIDE CHAIN:
โ€ข In addition to proteolytic processing (i.e., removal of the signal
peptide), the polypeptide is subject to other covalent
modifications:
N- and O-glycosylation and O-phosphorylation.
โ€ข After synthesis and transportation across the ER lumen, the
proteins pass to the Golgi apparatus and then, via secretory
vesicles, to the apical membrane.
โ€ข N-glycosylation - Asn-X-Thr/Ser (where X is any amino acid
except proline).
โ€ข O-glycosylation and O-phosphorylation - Ser/Thr-X-A
(where X is any amino acid residue and A is an acidic residue,
such as aspartic or glutamic acid or a phosphorylated amino
acid).
4. SECRETION OFIMMUNOGLOBULINS:
โ€ข The IgG of bovine colostrum is derived exclusively from blood
plasma.
โ€ข IgA in colostrum is derived partly from intra-mammary
synthesis and partly by accumulation in the gland after being
transported in the blood from other sites of synthesis.
The synthesis and secretion of milk proteins involves eight steps:
1. Transcription
2. Translation
3. Segregation
4. Modification
5. Concentration
6. Packaging
7. Storage
8. Exocytosis.
REFERENCES:
โ€ข Dairy chemistry and Biochemistry โ€“ P.F.FOX.

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Biosynthesis of milk proteins.pptx

  • 1. BIOSYNTHESIS OFMILK PROTEINS By R.KARTHIKA Ph.D student Department of Dairy Chemistry WEST BENGAL UNIVERSITY OF ANIMALAND FISHERY SCIENCES
  • 2. CONTENT: NO TITLE 1 SOUCES OF AMINO ACIDS 2 SYNTHESIS OF MILK PROTEINS 3 MODIFICATIONS OF POLYPEPTIDE CHAIN 4 SECRETION OF IMMUNOGLOBULINS 5 REFERENCES
  • 3. 1. SOUCESOF AMINO ACIDS 1. Synthesis โ€“ Blood plasma. Types of amino acids
  • 4. Contโ€ฆ. 2. Types of EAA: โ€ข EAA may be subdivided into those for which uptake from blood and output in milk proteins are almost exactly balanced (Group I). โ€ข Those for which uptake significantly exceeds output (Group 11). โ€ข Group 11 amino acids are metabolized in the mammary gland and provide amino groups, via transamination, for the biosynthesis of those amino acids for which uptake from blood is inadequate (Group Ill).
  • 5. โ€ข Group I amino acids: ๏ƒ˜methionine, ๏ƒ˜phenylalanine, ๏ƒ˜tyrosine, ๏ƒ˜Histidine ๏ƒ˜tryptophan. โ€ข Group II amino acids: o valine, o leucine, o isoleucine, olysine, o Arginine o threonine. โ€ข Group III amino acids: ๏ฑaspartic acid, ๏ฑglutamic acid, ๏ฑglycine, ๏ฑalanine, ๏ฑserine, ๏ฑcysteine/ cystine, ๏ฑproline
  • 6. 2. SYNTHESIS OF MILK PROTEINS โ€ข Synthesis of the major milk proteins occurs in the mammary gland. โ€ข Polymerization of the amino acids occurs on ribosomes fixed on the rough endoplasmic reticulum of the secretory cells, by the method common to all cells. โ€ข The primary blueprint for the amino acid sequence of proteins is contained in deoxyribonucleic acid (DNA) within the cell nucleus.
  • 7. CONTโ€ฆ โ€ข The requisite information is transcribed in the nucleus to ribonucleic acid (RNA) of which there are three types: โ€ข messenger RNA (mRNA) โ€ข transfer RNA (tRNA) โ€ข ribosomal RNA (rRNA) these are transferred to the cytoplasm where each plays a specific role in protein synthesis.
  • 8. โ€ข The specificity of the tRNAs is determined by the sequence of the anticodon. โ€ข Interaction between the tRNA and the appropriate amino acid occurs in the cytoplasm but the remaining reactions in protein synthesis occur in the ribosomes. โ€ข The ribosomes of animal cells have a diameter of about 22 nm and a sedimentation coefficient of 80S; they consist of two principal subunits: 60S and 40S.
  • 9. mRNA passes through a groove or tunnel between the 60S and 40S subunits; while in the groove, mRNA is protected from the action of ribonuclease.
  • 10. โ€ข The information for the amino acid sequence is contained in the mRNA. โ€ข Synthesis commences at the correct codon of the mRNA because a special amino acid derivative. โ€ข N-formyl methionine-is bound to a specific special codon and forms the temporary N-terminal residue of the protein. โ€ข N-formyl methionine is later hydrolysed off, together with a short hydrophobic signal peptide, exposing the permanent N-terminal residue. โ€ข The acyl amino acid-tRNA is bound to the mRNA just outside the ribosome by becoming attached to its corresponding codon.
  • 11. โ€ข Condensation is catalysed by a peptidyl transferase, which is part of the ribosomal subunit. โ€ข For the next cycle, a new acyl amino acid-tRNA is bound to the mRNA, the ribosome tracks along the mRNA and the vacated tRNA is ejected. โ€ข Termination of synthesis is controlled by a special ribosomally- bound protein, TB 3โ€“1, the protein release factor (RF) which recognises any of three โ€œstop codonsโ€ UAG, UAA and UGA.
  • 12. โ€ข Translocation through cell membranes is facilitated by a signal sequence, a sequence of 15โ€“29 amino acids at the amino terminal of the growing polypeptide chain. โ€ข This sequence causes the ribosome to bind to the ER membrane, in which a โ€˜channelโ€™ forms, allowing the growing chain to enter the ER lumen. โ€ข Subsequently, the signal sequence is cleaved from the polypeptide by a signal peptidase, an enzyme located on the luminal side of the ER membrane.
  • 13. 3. MODIFICATIONS OFTHE POLYPEPTIDE CHAIN: โ€ข In addition to proteolytic processing (i.e., removal of the signal peptide), the polypeptide is subject to other covalent modifications: N- and O-glycosylation and O-phosphorylation. โ€ข After synthesis and transportation across the ER lumen, the proteins pass to the Golgi apparatus and then, via secretory vesicles, to the apical membrane. โ€ข N-glycosylation - Asn-X-Thr/Ser (where X is any amino acid except proline). โ€ข O-glycosylation and O-phosphorylation - Ser/Thr-X-A (where X is any amino acid residue and A is an acidic residue, such as aspartic or glutamic acid or a phosphorylated amino acid).
  • 14. 4. SECRETION OFIMMUNOGLOBULINS: โ€ข The IgG of bovine colostrum is derived exclusively from blood plasma. โ€ข IgA in colostrum is derived partly from intra-mammary synthesis and partly by accumulation in the gland after being transported in the blood from other sites of synthesis.
  • 15. The synthesis and secretion of milk proteins involves eight steps: 1. Transcription 2. Translation 3. Segregation 4. Modification 5. Concentration 6. Packaging 7. Storage 8. Exocytosis.
  • 16.
  • 17.
  • 18. REFERENCES: โ€ข Dairy chemistry and Biochemistry โ€“ P.F.FOX.