BRENDA - Enzyme Database show
show all sequences of 1.14.11.4

Tissue-specific expression and regulation of the alternatively-spliced forms of lysyl hydroxylase 2 (LH2) in human kidney cells and skin fibroblasts

Walker, L.C.; Overstreet, M.A.; Yeowell, H.N.; Matrix Biol. 23, 515-523 (2005)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
genomic structure of isozyme LH2, expression analysis of the 2 splicing variants of isozyme LH2
Homo sapiens
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Homo sapiens
the long splicing variant of isozyme LH2 is the major ubiquitously-expressed form that is spliced into the short form, which is expressed together with the long form only in some tissues, e.g. kidney, spleen, liver, and placenta, alternative splicing can be regulated by both cell density and cycloheximide, regulation of LH2long transcript and of expression of both splicing variants in kidney via cycloheximide that suppress a factor taht inhibits exclusion of exon 13A thereby promoting expression of LH2short, and vice versa also via cycloheximide in fibroblasts, overview, perturbation of LH2 regulation can influence the stability of the extracellular matrix and contribute to connective tissue disorders
?
-
-
-
procollagen L-lysine + 2-oxoglutarate + O2
Homo sapiens
some hydroxylated L-lysine residues are precursors for the cross-link formation essential for the tensile strength of collagen, the 2 splicing variants exhibit different specificity for hydroxylation of either telopeptide or helical collagen domain lysine residues, so that their relative expression level determines the type of cross-links formed and affecting collagen strength
procollagen 5-hydroxy-L-lysine + succinate + CO2
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
O00469
2 splicing variants of isozyme LH2, termed LH2long and LH2short
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
aorta
expression only of LH2long
Homo sapiens
-
cartilage
expression of LH2long and LH2short
Homo sapiens
-
dura
expression only of LH2long
Homo sapiens
-
fibroblast
of skin, expression only of LH2long
Homo sapiens
-
HEK-293 cell
expression of LH2long and LH2short
Homo sapiens
-
kidney
expression of LH2long and LH2short
Homo sapiens
-
liver
expression of LH2long and LH2short
Homo sapiens
-
lung
expression only of LH2long
Homo sapiens
-
additional information
the long splicing variant of isozyme LH2 is the major ubiquitously-expressed form that is spliced into the short form, which is expressed together with the long form only in some tissues, e.g. kidney, cartilage, spleen, liver, and placenta, not in skin, lung, aorta, and dura
Homo sapiens
-
placenta
expression of LH2long and LH2short
Homo sapiens
-
skin
expression only of LH2long
Homo sapiens
-
spleen
expression of LH2long and LH2short
Homo sapiens
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the long splicing variant of isozyme LH2 is the major ubiquitously-expressed form that is spliced into the short form, which is expressed together with the long form only in some tissues, e.g. kidney, spleen, liver, and placenta, alternative splicing can be regulated by both cell density and cycloheximide, regulation of LH2long transcript and of expression of both splicing variants in kidney via cycloheximide that suppress a factor taht inhibits exclusion of exon 13A thereby promoting expression of LH2short, and vice versa also via cycloheximide in fibroblasts, overview, perturbation of LH2 regulation can influence the stability of the extracellular matrix and contribute to connective tissue disorders
659845
Homo sapiens
?
-
-
-
-
procollagen L-lysine + 2-oxoglutarate + O2
-
659845
Homo sapiens
procollagen 5-hydroxy-L-lysine + succinate + CO2
-
-
-
?
procollagen L-lysine + 2-oxoglutarate + O2
some hydroxylated L-lysine residues are precursors for the cross-link formation essential for the tensile strength of collagen, the 2 splicing variants exhibit different specificity for hydroxylation of either telopeptide or helical collagen domain lysine residues, so that their relative expression level determines the type of cross-links formed and affecting collagen strength
659845
Homo sapiens
procollagen 5-hydroxy-L-lysine + succinate + CO2
-
-
-
?
Cloned(Commentary) (protein specific)
Commentary
Organism
genomic structure of isozyme LH2, expression analysis of the 2 splicing variants of isozyme LH2
Homo sapiens
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Homo sapiens
the long splicing variant of isozyme LH2 is the major ubiquitously-expressed form that is spliced into the short form, which is expressed together with the long form only in some tissues, e.g. kidney, spleen, liver, and placenta, alternative splicing can be regulated by both cell density and cycloheximide, regulation of LH2long transcript and of expression of both splicing variants in kidney via cycloheximide that suppress a factor taht inhibits exclusion of exon 13A thereby promoting expression of LH2short, and vice versa also via cycloheximide in fibroblasts, overview, perturbation of LH2 regulation can influence the stability of the extracellular matrix and contribute to connective tissue disorders
?
-
-
-
procollagen L-lysine + 2-oxoglutarate + O2
Homo sapiens
some hydroxylated L-lysine residues are precursors for the cross-link formation essential for the tensile strength of collagen, the 2 splicing variants exhibit different specificity for hydroxylation of either telopeptide or helical collagen domain lysine residues, so that their relative expression level determines the type of cross-links formed and affecting collagen strength
procollagen 5-hydroxy-L-lysine + succinate + CO2
-
-
?
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
aorta
expression only of LH2long
Homo sapiens
-
cartilage
expression of LH2long and LH2short
Homo sapiens
-
dura
expression only of LH2long
Homo sapiens
-
fibroblast
of skin, expression only of LH2long
Homo sapiens
-
HEK-293 cell
expression of LH2long and LH2short
Homo sapiens
-
kidney
expression of LH2long and LH2short
Homo sapiens
-
liver
expression of LH2long and LH2short
Homo sapiens
-
lung
expression only of LH2long
Homo sapiens
-
additional information
the long splicing variant of isozyme LH2 is the major ubiquitously-expressed form that is spliced into the short form, which is expressed together with the long form only in some tissues, e.g. kidney, cartilage, spleen, liver, and placenta, not in skin, lung, aorta, and dura
Homo sapiens
-
placenta
expression of LH2long and LH2short
Homo sapiens
-
skin
expression only of LH2long
Homo sapiens
-
spleen
expression of LH2long and LH2short
Homo sapiens
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the long splicing variant of isozyme LH2 is the major ubiquitously-expressed form that is spliced into the short form, which is expressed together with the long form only in some tissues, e.g. kidney, spleen, liver, and placenta, alternative splicing can be regulated by both cell density and cycloheximide, regulation of LH2long transcript and of expression of both splicing variants in kidney via cycloheximide that suppress a factor taht inhibits exclusion of exon 13A thereby promoting expression of LH2short, and vice versa also via cycloheximide in fibroblasts, overview, perturbation of LH2 regulation can influence the stability of the extracellular matrix and contribute to connective tissue disorders
659845
Homo sapiens
?
-
-
-
-
procollagen L-lysine + 2-oxoglutarate + O2
-
659845
Homo sapiens
procollagen 5-hydroxy-L-lysine + succinate + CO2
-
-
-
?
procollagen L-lysine + 2-oxoglutarate + O2
some hydroxylated L-lysine residues are precursors for the cross-link formation essential for the tensile strength of collagen, the 2 splicing variants exhibit different specificity for hydroxylation of either telopeptide or helical collagen domain lysine residues, so that their relative expression level determines the type of cross-links formed and affecting collagen strength
659845
Homo sapiens
procollagen 5-hydroxy-L-lysine + succinate + CO2
-
-
-
?
Other publictions for EC 1.14.11.4
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
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2
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2
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746479
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746171
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1
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2
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3
3
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745323
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1
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4
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2
2
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745334
Gjaltema
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Homo sapiens
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290
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1
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1
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1
1
1
1
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745431
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3
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1
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3
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5
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7
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3
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2
1
3
3
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745445
Chen
Lysyl hydroxylase 2 induces a ...
Homo sapiens, Mus musculus
J. Clin. Invest.
125
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2015
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1
2
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2
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2
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4
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9
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1
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2
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9
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2
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3
3
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745769
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399
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1
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1
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2
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1
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6
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9
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3
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3
9
-
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746253
Risteli
Lysyl hydroxylase 3 modifies ...
Mus musculus, Mus musculus C57BL/6
PLoS ONE
9
e113498
2014
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1
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6
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8
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2
2
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724702
Remst
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Homo sapiens
Cell Tissue Res.
355
163-171
2013
-
1
1
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2
1
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724792
Tsukamoto
Cloning and expression of cDNA ...
Takifugu rubripes
Comp. Biochem. Physiol. B
166
123-132
2013
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15
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44
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3
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3
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1
3
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725955
Gilkes
Procollagen lysyl hydroxylase ...
Homo sapiens
Mol. Cancer Res.
11
456-466
2013
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1
1
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722865
Wang
Lysyl hydroxylase 3 is secrete ...
Canis lupus familiaris, Canis lupus familiaris Madin-Darby, Homo sapiens
J. Cell. Physiol.
227
668-675
2012
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1
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1
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725865
Mantri
-
Self-hydroxylation of the spli ...
Homo sapiens
MedChemComm
3
80-85
2012
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726309
Ruotsalainen
The activities of lysyl hydrox ...
Mus musculus, Mus musculus C57BL/6
PLoS ONE
7
e50045
2012
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2
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142
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2
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725092
Bunt
Characterisation of the Drosop ...
Drosophila melanogaster
Gene Expr. Patterns
11
72-78
2011
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1
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2
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725453
Luther
Mimivirus collagen is modified ...
Acanthamoeba polyphaga Mimivirus, Acanthamoeba polyphaga Mimivirus L230
J. Biol. Chem.
286
43701-43709
2011
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8
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725464
Sricholpech
Lysyl hydroxylase 3 glucosylat ...
Mus musculus, Mus musculus CRL-2593
J. Biol. Chem.
286
8846-8856
2011
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439164
Valtavaara
Cloning and characterization o ...
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6831-6834
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1
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439169
Armstrong
Rat lysyl hydroxylase: molecul ...
Gallus gallus, Homo sapiens, Rattus norvegicus
Biochim. Biophys. Acta
1264
93-102
1995
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2
1
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6
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3
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4
1
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439163
Kellokumpu
Lysyl hydroxylase, a collagen ...
Homo sapiens
J. Biol. Chem.
269
30524-30529
1994
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1
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349014
Majamaa
Differences between collagen h ...
Gallus gallus
Biochem. J.
229
127-133
1985
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439151
Royce
Failure of highly purified lys ...
Gallus gallus
Biochem. J.
230
475-480
1985
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1
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439149
Kivirikko
Posttranslational enzymes in t ...
Gallus gallus, Homo sapiens
Methods Enzymol.
82
245-304
1982
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8
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2
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2
2
2
1
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2
2
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439150
Puistola
Catalytic properties of lysyl ...
Gallus gallus, Homo sapiens
Biochem. J.
201
215-219
1982
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7
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439148
Kivirikko
-
The hydroxylation of prolyl an ...
Gallus gallus
Enzymol. Post- transl. Modif. Proteins (Freedman, R. B. , Hawkins, H. C. , eds. ) Academic Press, New York
1
53-104
1980
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439152
Puistola
Studies on the lysyl hydroxyla ...
Gallus gallus
Biochim. Biophys. Acta
611
40-50
1980
4
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439153
Puistola
Studies on the lysyl hydroxyla ...
Gallus gallus
Biochim. Biophys. Acta
611
51-60
1980
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8
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439154
Turpeenniemi-Hujanen
Isolation of lysyl hydroxylase ...
Gallus gallus
Biochem. J.
189
247-253
1980
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439155
Miller
-
Purification and enzymatic pro ...
Sus scrofa
Biochemistry
18
5928-5932
1979
3
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3
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439156
Murray
Inhibition of lysyl hydroxylas ...
Gallus gallus
Biochim. Biophys. Acta
481
63-70
1977
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11
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439157
Ryhänen
Lysyl hydroxylase. Further pur ...
Gallus gallus
Biochim. Biophys. Acta
438
71-89
1976
3
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5
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439158
Kivirikko
Studies on protocollagen lysin ...
Gallus gallus
Biochemistry
11
122-129
1972
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3
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439159
Popenoe
Partial purification and prope ...
Gallus gallus
Biochim. Biophys. Acta
258
380-386
1972
2
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439160
Kivirikko
Partial purification and chara ...
Gallus gallus
Biochim. Biophys. Acta
258
366-379
1972
3
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439162
Hausmann E.
Cofactor requirements for the ...
Gallus gallus
Biochim. Biophys. Acta
133
591-593
1967
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