JPH0529430B2 - - Google Patents

Info

Publication number: JPH0529430B2
Authority: JP; Japan
Prior art keywords: lysozyme; substituted; reduced; reduced lysozyme; alkylated
Prior art date: 1984-12-28
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.): Expired - Lifetime

Application number

JP27786584A

Other languages

English (en)

Japanese (ja)

Other versions

JPS61268181A (ja

Inventor

Taiji Imoto

Hidenori Yamada

Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)

Individual

Original Assignee

Individual

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

1984-12-28

Filing date

1984-12-28

Publication date

1993-04-30

1984-12-28 Application filed by Individual filed Critical Individual

1984-12-28 Priority to JP27786584A priority Critical patent/JPS61268181A/ja

1986-11-27 Publication of JPS61268181A publication Critical patent/JPS61268181A/ja

1993-04-30 Publication of JPH0529430B2 publication Critical patent/JPH0529430B2/ja

Status Granted legal-status Critical Current

Links

235000010335 lysozyme Nutrition 0.000 claims description 70
102000016943 Muramidase Human genes 0.000 claims description 69
108010014251 Muramidase Proteins 0.000 claims description 69
108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 claims description 69
229960000274 lysozyme Drugs 0.000 claims description 69
239000004325 lysozyme Substances 0.000 claims description 69
239000002168 alkylating agent Substances 0.000 claims description 11
229940100198 alkylating agent Drugs 0.000 claims description 11
125000003396 thiol group Chemical group [H]S* 0.000 claims description 11
NNZGNZHUGJAKKT-UHFFFAOYSA-M 3-bromopropyl(trimethyl)azanium;bromide Chemical group [Br-].C[N+](C)(C)CCCBr NNZGNZHUGJAKKT-UHFFFAOYSA-M 0.000 claims description 9
238000004519 manufacturing process Methods 0.000 claims description 8
-1 dimethylaminoethyl group Chemical group 0.000 claims description 6
JDNTWHVOXJZDSN-UHFFFAOYSA-N iodoacetic acid Chemical group OC(=O)CI JDNTWHVOXJZDSN-UHFFFAOYSA-N 0.000 claims description 4
MFRUVSDIZTZFFL-UHFFFAOYSA-N 2-bromo-n,n-dimethylethanamine;hydrobromide Chemical group [Br-].C[NH+](C)CCBr MFRUVSDIZTZFFL-UHFFFAOYSA-N 0.000 claims description 3
WJAXXWSZNSFVNG-UHFFFAOYSA-N 2-bromoethanamine;hydron;bromide Chemical group [Br-].[NH3+]CCBr WJAXXWSZNSFVNG-UHFFFAOYSA-N 0.000 claims description 3
OINMNSFDYTYXEQ-UHFFFAOYSA-M 2-bromoethyl(trimethyl)azanium;bromide Chemical group [Br-].C[N+](C)(C)CCBr OINMNSFDYTYXEQ-UHFFFAOYSA-M 0.000 claims description 3
PGLTVOMIXTUURA-UHFFFAOYSA-N iodoacetamide Chemical group NC(=O)CI PGLTVOMIXTUURA-UHFFFAOYSA-N 0.000 claims description 2
125000000022 2-aminoethyl group Chemical group [H]C([*])([H])C([H])([H])N([H])[H] 0.000 claims 1
125000002057 carboxymethyl group Chemical group [H]OC(=O)C([H])([H])[*] 0.000 claims 1
150000001413 amino acids Chemical class 0.000 description 15
235000001014 amino acid Nutrition 0.000 description 13
235000018417 cysteine Nutrition 0.000 description 12
108091005804 Peptidases Proteins 0.000 description 11
102000035195 Peptidases Human genes 0.000 description 11
239000004365 Protease Substances 0.000 description 11
108090000765 processed proteins & peptides Proteins 0.000 description 10
238000006243 chemical reaction Methods 0.000 description 9
XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 9
239000000243 solution Substances 0.000 description 9
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 9
KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 8
239000004472 Lysine Substances 0.000 description 8
238000004458 analytical method Methods 0.000 description 8
102000004142 Trypsin Human genes 0.000 description 7
108090000631 Trypsin Proteins 0.000 description 7
239000012588 trypsin Substances 0.000 description 7
NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 6
102000004196 processed proteins & peptides Human genes 0.000 description 6
239000000758 substrate Substances 0.000 description 6
238000005804 alkylation reaction Methods 0.000 description 5
239000003638 chemical reducing agent Substances 0.000 description 5
235000014113 dietary fatty acids Nutrition 0.000 description 5
229930195729 fatty acid Natural products 0.000 description 5
239000000194 fatty acid Substances 0.000 description 5
125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 4
150000001945 cysteines Chemical class 0.000 description 4
235000018102 proteins Nutrition 0.000 description 4
102000004169 proteins and genes Human genes 0.000 description 4
108090000623 proteins and genes Proteins 0.000 description 4
QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
102000004877 Insulin Human genes 0.000 description 3
108090001061 Insulin Proteins 0.000 description 3
QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 3
LEVWYRKDKASIDU-IMJSIDKUSA-N L-cystine Chemical compound [O-]C(=O)[C@@H]([NH3+])CSSC[C@H]([NH3+])C([O-])=O LEVWYRKDKASIDU-IMJSIDKUSA-N 0.000 description 3
235000004279 alanine Nutrition 0.000 description 3
230000029936 alkylation Effects 0.000 description 3
229960003067 cystine Drugs 0.000 description 3
229940125396 insulin Drugs 0.000 description 3
DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 3
XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 2
238000004040 coloring Methods 0.000 description 2
230000029087 digestion Effects 0.000 description 2
150000004665 fatty acids Chemical class 0.000 description 2
238000010438 heat treatment Methods 0.000 description 2
230000007062 hydrolysis Effects 0.000 description 2
238000006460 hydrolysis reaction Methods 0.000 description 2
230000003301 hydrolyzing effect Effects 0.000 description 2
125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 2
FEMOMIGRRWSMCU-UHFFFAOYSA-N ninhydrin Chemical compound C1=CC=C2C(=O)C(O)(O)C(=O)C2=C1 FEMOMIGRRWSMCU-UHFFFAOYSA-N 0.000 description 2
230000006207 propylation Effects 0.000 description 2
238000004007 reversed phase HPLC Methods 0.000 description 2
238000007086 side reaction Methods 0.000 description 2
KZLYQYPURWXOEW-UHFFFAOYSA-N 2-iodopropanoic acid Chemical compound CC(I)C(O)=O KZLYQYPURWXOEW-UHFFFAOYSA-N 0.000 description 1
QCVGEOXPDFCNHA-UHFFFAOYSA-N 5,5-dimethyl-2,4-dioxo-1,3-oxazolidine-3-carboxamide Chemical compound CC1(C)OC(=O)N(C(N)=O)C1=O QCVGEOXPDFCNHA-UHFFFAOYSA-N 0.000 description 1
239000004475 Arginine Substances 0.000 description 1
BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 1
102000002322 Egg Proteins Human genes 0.000 description 1
108010000912 Egg Proteins Proteins 0.000 description 1
HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 1
MQUQNUAYKLCRME-INIZCTEOSA-N N-tosyl-L-phenylalanyl chloromethyl ketone Chemical compound C1=CC(C)=CC=C1S(=O)(=O)N[C@H](C(=O)CCl)CC1=CC=CC=C1 MQUQNUAYKLCRME-INIZCTEOSA-N 0.000 description 1
229920005654 Sephadex Polymers 0.000 description 1
239000012507 Sephadex™ Substances 0.000 description 1
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 1
239000007983 Tris buffer Substances 0.000 description 1
101710119636 Trypsin-5 Proteins 0.000 description 1
239000002253 acid Substances 0.000 description 1
239000003929 acidic solution Substances 0.000 description 1
230000002152 alkylating effect Effects 0.000 description 1
SWLVFNYSXGMGBS-UHFFFAOYSA-N ammonium bromide Chemical compound [NH4+].[Br-] SWLVFNYSXGMGBS-UHFFFAOYSA-N 0.000 description 1
239000007864 aqueous solution Substances 0.000 description 1
ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
238000009835 boiling Methods 0.000 description 1
239000000872 buffer Substances 0.000 description 1
239000007853 buffer solution Substances 0.000 description 1
239000004202 carbamide Substances 0.000 description 1
229940096384 chicken egg white lysozyme Drugs 0.000 description 1
238000003776 cleavage reaction Methods 0.000 description 1
238000007796 conventional method Methods 0.000 description 1
238000010411 cooking Methods 0.000 description 1
125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 1
238000007865 diluting Methods 0.000 description 1
239000012153 distilled water Substances 0.000 description 1
150000002019 disulfides Chemical class 0.000 description 1
230000000694 effects Effects 0.000 description 1
210000000969 egg white Anatomy 0.000 description 1
235000014103 egg white Nutrition 0.000 description 1
238000010828 elution Methods 0.000 description 1
WBJINCZRORDGAQ-UHFFFAOYSA-N ethyl formate Chemical compound CCOC=O WBJINCZRORDGAQ-UHFFFAOYSA-N 0.000 description 1
DNJIEGIFACGWOD-UHFFFAOYSA-N ethyl mercaptane Natural products CCS DNJIEGIFACGWOD-UHFFFAOYSA-N 0.000 description 1
229940071106 ethylenediaminetetraacetate Drugs 0.000 description 1
125000002795 guanidino group Chemical group C(N)(=N)N* 0.000 description 1
HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
125000000487 histidyl group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C([H])=N1 0.000 description 1
239000007788 liquid Substances 0.000 description 1
125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
239000012528 membrane Substances 0.000 description 1
239000000203 mixture Substances 0.000 description 1
230000007935 neutral effect Effects 0.000 description 1
IJGRMHOSHXDMSA-UHFFFAOYSA-N nitrogen Substances N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 1
229910052757 nitrogen Inorganic materials 0.000 description 1
QJGQUHMNIGDVPM-UHFFFAOYSA-N nitrogen group Chemical group [N] QJGQUHMNIGDVPM-UHFFFAOYSA-N 0.000 description 1
231100000957 no side effect Toxicity 0.000 description 1
229920001184 polypeptide Polymers 0.000 description 1
230000035484 reaction time Effects 0.000 description 1
239000012266 salt solution Substances 0.000 description 1
150000003839 salts Chemical class 0.000 description 1
230000007017 scission Effects 0.000 description 1
230000020509 sex determination Effects 0.000 description 1
125000000547 substituted alkyl group Chemical group 0.000 description 1
PXQLVRUNWNTZOS-UHFFFAOYSA-N sulfanyl Chemical compound [SH] PXQLVRUNWNTZOS-UHFFFAOYSA-N 0.000 description 1
LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1

Landscapes

Enzymes And Modification Thereof (AREA)

JP27786584A 1984-12-28 1984-12-28 Ｓ−置換アルキル化還元リゾチ−ムおよびその製造方法 Granted JPS61268181A (ja)

Priority Applications (1)

Application Number	Priority Date	Filing Date	Title
JP27786584A JPS61268181A (ja)	1984-12-28	1984-12-28	Ｓ−置換アルキル化還元リゾチ−ムおよびその製造方法

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
JP27786584A JPS61268181A (ja)	1984-12-28	1984-12-28	Ｓ−置換アルキル化還元リゾチ−ムおよびその製造方法

Publications (2)

Publication Number	Publication Date
JPS61268181A JPS61268181A (ja)	1986-11-27
JPH0529430B2 true JPH0529430B2 (fr)	1993-04-30

Family

ID=17589360

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
JP27786584A Granted JPS61268181A (ja)	1984-12-28	1984-12-28	Ｓ−置換アルキル化還元リゾチ−ムおよびその製造方法

Country Status (1)

Country	Link
JP (1)	JPS61268181A (fr)

Families Citing this family (1)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
DE3708499A1 (de) *	1987-03-16	1988-10-20	Sgs Halbleiterbauelemente Gmbh	Digitale gegentakt-treiberschaltung

1984
- 1984-12-28 JP JP27786584A patent/JPS61268181A/ja active Granted

Also Published As

Publication number	Publication date
JPS61268181A (ja)	1986-11-27

Publication	Publication Date	Title
Gurd	1967	[62] Carboxymethylation
Brew et al.	1970	The complete amino acid sequence of bovine α-lactalbumin
Ishiura et al.	1978	Studies of a calcium-activated neutral protease from chicken skeletal muscle: I. Purification and characterization
Kimmel	1967	[70] Guanidination of proteins
Yoshimoto et al.	1983	Post-proline cleaving enzyme (prolyl endoeptidase) from bovine brain
CA2142780C (fr)	2008-10-14	Methode de preparation d'insuline possedant des ponts cystine a des positions strategiques
Phillips	1958	The N-terminal groups of calf-thymus histones
JP2592981B2 (ja)	1997-03-19	タンパク質アミノ末端配列の酸素的除去
JANDER et al.	1981	A Cysteine‐Rich Collagenous Protein from Bovine Placenta: Isolation of Its Constituent Polypeptide Chains and Some Properties of the Non‐denatured Protein
Shapira et al.	1971	Encephalitogenic fragment of myelin basic protein: amino acid sequence of bovine, rabbit, guinea pig, monkey, and human fragments
JPH02131594A (ja)	1990-05-21	デ‐ｂ３０‐インシュリンおよびデ‐ｂ３０‐インシュリン誘導体の製造方法
Zick et al.	1982	Interchain disulfide bonding in the regulatory subunit of cAMP-dependent protein kinase I.
Vacher-Lepretre et al.	1976	Study of the apoprotein of Folch-Pi bovine proteolipid. II. Characterization of the components isolated from sodium dodecyl sulfate solutions
Hofmann	1964	The purification and properties of fragments of trypsinogen obtained by cyanogen bromide cleavage
JPS642360B2 (fr)	1989-01-17
Riley et al.	1970	The reversible reaction of protein amino groups with exo-cis-3, 6-endoxo-Δ4-tetrahydrophthalic anhydride. The reaction with lysozyme
Okazaki et al.	1985	A convenient protein substrate for the determination of protease specificity: reduced and S-3-(trimethylated amino) propylated lysozyme
Groves et al.	1963	Isolation, characterization, and amino acid composition of a new crystalline protein, lactollin, from milk
Lejeune et al.	1983	Amino acid sequence around a hormonogenic tyrosine residue in the N-terminal region of human thyroglobulin after in vivo and in vitro iodination
Liu et al.	1979	Studies on Limulus lysate coagulating system
Qian et al.	1984	Separation and characterization of two polypeptide chains from the 7S cross-linking domain of basement-membrane (type IV) collagen
Barman	1972	The modification of the tryptophan residues of bovine α-lactalbumin with 2-hydroxy-5-nitrobenzyl bromide and with dimethyl (2-hydroxy-5-nitrobenzyl) sulphonium bromide. I. Characterisation of the modified protein
JPH0529430B2 (fr)	1993-04-30
Friedman et al.	1975	Reactions of proteins with ethyl vinyl sulfone
Minuth et al.	1978	The phenoloxidases of the ascomycete Podospora anserina: structural differences between laccases of high and low molecular weight