Search Results - "Jabusch, J R"

The sequence of equine muscle carbonic anhydrase by Wendorff, K M, Nishita, T, Jabusch, J R, Deutsch, H F

“…The sequence of equine muscle carbonic anhydrase (CA-III) has been determined. The 2 reactive cysteines of the 5 such residues have been localized. A strong…”
Get full text

Sequence of the low activity equine erythrocyte carbonic anhydrase and delineation of the amino acid substitutions in various polymorphic forms by Jabusch, J R, Bray, R P, Deutsch, H F

“…the sequence of the low activity form of equine erythrocyte carbonic anhydrase has been determined. The most common electrophoretic form, designated D, has…”
Get full text

Purification and properties of a polymorphic high activity equine erythrocyte carbonic anhydrase by Deutsch, H F, Jabusch, J R, Lin, K T

“…A polymorphic form of the high activity or C-type of horse erythrocyte carbonic anhydrase has been isolated. It has been designated C2 and differs from the…”
Get full text

Localization of lysines acetylated in ubiquitin reacted with p-nitrophenyl acetate by Jabusch, J R, Deutsch, H F

“…The protein ubiquitin undergoes extensive N epsilon-acetylation of some of its seven lysine residues when reacted with p-nitrophenyl acetate. Lysines 27 and 29…”
Get more information

Sequence of the high-activity equine erythrocyte carbonic anhydrase: N-terminal polymorphism (acetyl-Ser/acetyl-Thr) and homologies to similar mammalian isozymes by JABUSCH, J. R, DEUTSCH, H. F

“…The amino acid sequence of the high-activity equine erythrocyte carbonic anhydrase (CA-II) has been determined. Two different N-termini are noted, the C1 form…”
Get full text

The effect of thiodiglycol and dithiothreitol on the alkaline hydrolysis products of certain amino acid phenylthiohydantoins by Jabusch, J R, Parmelee, D C, Deutsch, H F

“…The thiazolinone and phenylthiohydantoin derivatives of most amino acids can be hydrolyzed with alkaline dithionite to generate the free amino acid. The…”
Get more information

Some sulfhydryl properties and primary structure of human erythrocyte superoxide dismutase by Jabusch, J R, Farb, D L, Kerschensteiner, D A, Deutsch, H F

“…Human Cu-Zn superoxide dismutase prepared by different methods shows varying properties relevant to its sulfhydryl chemistry. A cysteine residue not found in…”
Get full text

Primary structure of a human lambda-chain (Weir) of the Mcg type by Jabusch, J R, Deutsch, H F

“…The amino acid sequence of the Bence-Jones protein Weir has been determined. This lambda II protein is of the Mcg type. Since a mixed dinner of Weir and Mcg…”
Get more information

Isolation and crystallization of ubiquitin from mature erythrocytes by Jabusch, J R, Deutsch, H F

“…A relatively simple and reproducible procedure for the isolation of the active form of ubiquitin has been developed. The amount of this protein in mature…”
Get more information