Modification of the substrate specificity of porcine pepsin for the enzymatic production of bovine hide gelatin.

about

The evolution of pepsinogen C genes in vertebrates: duplication, loss and functional diversification Extraction of gelatin from salmon (Salmo salar) fish skin using trypsin-aided process: optimization by Plackett-Burman and response surface methodological approaches.

P2860

Q28731409-0117189E-BC8D-4CAE-A048-AB8FEAC36B78 Q47397723-40CFF40F-5917-4370-BB16-3E837A5AFB36

P2860

Modification of the substrate specificity of porcine pepsin for the enzymatic production of bovine hide gelatin.

Item

http://www.wikidata.org/entity/Q42847374

description

2000 nî lūn-bûn

@nan

2000年の論文

@ja

2000年論文

@yue

2000年論文

@zh-hant

2000年論文

@zh-hk

2000年論文

@zh-mo

2000年論文

@zh-tw

2000年论文

@wuu

2000年论文

@zh

2000年论文

@zh-cn

name

Modification of the substrate ...... uction of bovine hide gelatin.

@en

Modification of the substrate ...... uction of bovine hide gelatin.

@nl

type

Item

label

Modification of the substrate ...... uction of bovine hide gelatin.

@en

Modification of the substrate ...... uction of bovine hide gelatin.

@nl

prefLabel

Modification of the substrate ...... uction of bovine hide gelatin.

@en

Modification of the substrate ...... uction of bovine hide gelatin.

@nl

P1476

Modification of the substrate ...... uction of bovine hide gelatin.

@en

P2093

Blakeley R

http://www.w3.org/2001/XMLSchema#string

Dalrymple BP

http://www.w3.org/2001/XMLSchema#string

Galea CA

http://www.w3.org/2001/XMLSchema#string

Kuypers R

http://www.w3.org/2001/XMLSchema#string

P2860

Crystal structures of native and inhibited forms of human cathepsin D: implications for lysosomal targeting and drug design

Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes

Crystal structure of human pepsin and its complex with pepstatin

Structure of a pepsin/renin inhibitor complex reveals a novel crystal packing induced by minor chemical alterations in the inhibitor

X-ray analyses of aspartic proteinases. IV. Structure and refinement at 2.2 A resolution of bovine chymosin

The three-dimensional structure of recombinant bovine chymosin at 2.3 A resolution

X-ray analysis at 2.0 A resolution of mouse submaxillary renin complexed with a decapeptide inhibitor CH-66, based on the 4-16 fragment of rat angiotensinogen

On the size of the active site in proteases. I. Papain

Isolation and characterization of a stable activation intermediate of the lysosomal aspartyl protease cathepsin D

Mode of inhibition of acid proteases by pepstatin

P304

1947-1959

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1110/PS.9.10.1947

http://www.w3.org/2001/XMLSchema#string

P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P577

2000-10-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

12222228

http://www.w3.org/2001/XMLSchema#string

P698

11106168

http://www.w3.org/2001/XMLSchema#string

P932

2144476

http://www.w3.org/2001/XMLSchema#string

Modification of the substrate specificity of porcine pepsin for the enzymatic production of bovine hide gelatin.

about

P2860

P2860

Modification of the substrate specificity of porcine pepsin for the enzymatic production of bovine hide gelatin.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P5875

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P5875

P698

P932