Atlas of protein spectra in the ultraviolet and visible regions, volume 2 (1974)

EXPERIMENTAL CONDITIONS AND COMMENTS Solvent: NAME: Acetolactate-forxning Enzyme pH 6 SOURCE: Aerobacter aerogenes a bacterium REFERENCE: F.C.. EXPERIMENTAL CONDITIONS AND COMMENTS Solve

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Atlas of Protein Spectra in the Ultraviolet and Visible Regions

Volume 2

Edited by Donald M Kirschenbaum, Ph D.

Associate Professor

Department of Biochemistry

College of Medicine and School of Graduate Studies

Downstate Medical Center State University of New York Brooklyn, New York

IFI/PLENUM • NEWYORK-WASHINGTON-LONDON

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Library of Congress Catalog Card Number 77-183566

ISBN 0-306-67302-9

A Subsidiary of Plenum Publishing Corporation

227 West 17th Street, New York, N.Y 10011 United Kingdom edition published by Plenum Press, London

A Division of Plenum Publishing Company, Ltd.

Davis House (4th Floor), 8 Scrubs Lane, Harlesden, NWlO 6SE, London, England

No part of this publication may be reproduced in any form

without written permission from the publisher

Printed in the United States of America

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To Roslyn

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11He who ascribes a citation unto its author brings redemption into the world."

Ethics of the Fathers, Megilla 15, Rabbi Elazar citing Rabbi HaninaPermission to publish the figures used in this book has been obtained from the editors,publishers, and, where necessary, authors, of the material cited in the following journalsand books:

Journals

Acta Biochimica et Biophysica Academiae Scientiarum Hungaricae

Acta Biologica et Medica Germanica

Acta Chemica Scandinavica

Acta Endocrinologica

Advances in Clinical Chemistry

Advances in Protein Chemistry

Agricultural and Biological Chemistry

American Journal of Opt halmo logy

American Journal of Physiology

Analytical Biochemistry

Archives of Biochemistry and Biophysics

Archiv fur die Gesamte Virusforschung

Biochimica Biophysica Acta

Biochimica Biophysica Acta Library

Biochemical and Biophysical Research Communications

The Biochemical Journal

Biochemische Zeitschrift/European Journal of Biochemistry

Biochemistry

Biochemistry (Biokhimya)

Biophysik

Bulletin of the Agricultural Chemical Society of Japan

Bulletin of the Japanese Society of Scientific Fisheries

Bulletin de Ia Societe de Chimie Biologique

Canadian Journal of Biochemistry

Chemische Berichte/Berichte der Deutschen Chemischen Gesellschaft

Clinica Chimica Acta

Cold Spring Harbor Symposium on Quantitative Biology

Collection Czechoslovak Chemical Communications

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Comparative Biochemistry and Physiology

Comptes rendus Academie Science, Paris

Comptes rendus des travaux du Laboratoire Carlsberg

Hoppe-Seyler's Zeitschrift fur Physiologische Chemie

International Archives of Allergy and Applied Immunology

International Journal of Protein Research

International Journal of Radiation Biology

Journal of Agricultural and Food Chemistry

Journal of the American Chemical Society

Journal of Bacteriology

Journal of Biochemistry, Tokyo

Journal of Biological Chemistry

Journal of Biophysical and Biochemical Cytology

Journal of Clinical Investigation

Journal of Experimental Medicine

Journal of General Virology

Journal of Histochemistry and Cytochemistry

Journal of Immunology

Journal of Laboratory and Clinical Medicine

Journal of Lipid Research

Journal of Molecular Biology

Proceedings of the Academy of Sciences, USSR (Doklady Akademii Nauk SSSR)

Proceedings of the Koninklijke Nederlandse Akademie van Wetenschappen

Proceedings of the National Academy of Sciences, USA

Proceedings of the Royal Society of London

Biological and Chemical Aspects of Oxygenases (Eds K Bloch and O Hayaishi)Tokyo; Maruzen Co Ltd., 1966

C02: Chemical, Biochemical and Physiological Aspects (Eds R Forster, J Edsall,

A Otis, and F Roughton) NASA SP-188 Washington, D C., 1969

The Haemostatic Mechanism in Man and Other Animals; the proceedings of a symposium.(Ed R MacFarlane) New York-London; Academic Press, Inc., 1970 (Symposia ofthe Zoological Society of London, No 27)

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Metabolic Regulation and Enzyme Action FEES proceedings of the 6th meeting, Madrid.(Eds A Sols and S Grisolia) New York; Academic Press, Inc., 1970 (FEESSymposia, Volume 19).

Non-Heme Iron Proteins: Role in energy conversions (Ed A San Pietro) YellowSprings, Ohio; Antioch Press, 1965

Prebiotic and Biochemical Evolution (Eds A Kimball and J Oro) New York, AmericanElsevier Pub Co., 1971

Probes of Structure and Function of Macromolecules and Membranes Volume 2: Probes

of enzyme and hemoproteins (Ed B Chance) New York, Academic Press, Inc.,1971

!Proceedings of the 7th Congress European Society of Hematology Part II/2 NewYork-London; S Karger, 1959-

Pyridine NucIeotide-Dependent Dehydrogenases (Ed H Sund) New York; SpringerVerlag, 1970

Specificity of Cell Surfaces (Eds B Davis and L Warren) New Jersey; Hall, Inc., 1967

Prentice-The Svedberg (Eds A Tiselius and K Pedersen) Uppsala; Almquist and WiksallBoktryckeri A B., 19Wj-

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I have gathered a bouquet of flowers from other men's gardens; naught but the string that binds them is my own.

Montaigne

PREFACE

The format of this volume is similar to that of Volume 1 In this volume there are approximately 1150 spectra of proteins obtained under a variety of conditions This is twice the number of spectra found in Volume 1 .For each figure, the source of the protein and the conditions under which the spectrum was taken are given if supplied by the original reference None of the spectrophotometric parameters so dear to spectroscopists are given

as they were not given in the original references Unless otherwise stated, the spectra were taken of solutions in a 1-cm cell.

Approximately 8% of the references are to work published prior to 1960, 12% are for

1960-1965, 20/0 for 1966-1969, 27/o for 1970, 30/o for 1971, and 3$ for 1972; thus some 80/o of the references are to the literature covering the period from 1966 to early 1972.

The spectra are arranged alphabetically and cross-indexed by source: animal, tissue, microbial, viral, plant and algae, yeast and fungi, and apoproteins There is also an index to those additives or modifiers which change the spectra of the proteins, e.g., a given protein and its nitro-derivative, or a given protein and the effect of a certain solvent upon its spectrum.

This volume and its predecessor should prove useful to anyone interested in protein spectra Specific examples of possible uses include the following: a protein chemist who desires to compare the spectrum taken in the 1950 Ts with that of the spectrum of the same protein taken in the 1970*s; a hematologist who wishes to see the spectral differences among different hemoglobins; a researcher with the spectrum of a protein he has recently isolated who desires to compare some of its odd spectral features with spectra in these volumes; and a student who desires to know what kind of spectra proteins have in different solvents.

Standard abbreviations have been used in this volume and it has been assumed that readers know what they stand for The abbreviations used in the original references have been retained; thus DPN and DPNH, TPN and TPNH, NAD and NADH, and NADP and NADPH have been used, as well as AMP and ATP.

The Library of the Downstate Medical Center has been the major source of the necessary journals and books What they didnrt have available, they went out of their way to try and obtain for me During the summer months of 1971 and 1972 the Library of the Marine Bio- logical Laboratory, Woods Hole, Massachusetts, was my "library-away-from-the-library." Here I was able to examine many of the nonmedical journals and books I should like to thank the librarians and staff of both libraries for their very necessary assistance.

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I should also like to thank Mrs E Bakker for help in preparing the figures forpublication; Miss M Colindreler for typing the indexes; Mrs E Levine for photocopying

•work; and Mr W Kratil for photographing the figures

If there are any errors I am responsible for them and I would appreciate having thembrought to my attention

Donald M Kirschenbaum

Downstate Medical Center

Brooklyn, New York

1973

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xiii This page has been reformatted by Knovel to provide easier navigation

Contents

Acknowledgments vii

Preface xii

Protein Spectra: A 1

ACE 1

ACO 2

ACY 3

ADE 4

ALB 7

ALD 21

AMI 27

AMY 53

ANA 55

ANG 56

ARA 57

ARG 58

ARO 61

ASP 62

ATP 64

AZU 65

Protein Spectra: B 66

BAC 66

Protein Spectra: C 69

CAR 69

CAT 81

CEL 83

CER 84

CHL 85

CHR 87

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xiv Contents

This page has been reformatted by Knovel to provide easier navigation

CHY 90

COB 92

CON 93

CRY 95

CYC 98

CYS 99

CYT 104

Protein Spectra: D 172

DEO 172

DIM 173

DIP 174

DPN 175

Protein Spectra: E 176

ELA 176

ERA 177

ERY 179

Protein Spectra: F 181

FAC 181

FAT 182

FER 183

FIB 194

FLA 195

FRU 203

Protein Spectra: G 204

GAL 204

GEL 205

GLU 207

GLY 225

Protein Spectra: H 233

HAP 233

HEM 234

HEX 293

HIS 295

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Contents xv

This page has been reformatted by Knovel to provide easier navigation HOM 304

HOR 306

HYD 307

Protein Spectra: I 310

IMI 310

INS 313

Protein Spectra: K 315

KYN 315

Protein Spectra: L 317

LAC 317

LEG 325

LEU 329

LIP 331

LUC 345

LYS 347

Protein Spectra: M 355

MAC 355

MAL 356

MEA 357

MEM 358

MER 361

MET 362

MIC 365

MOL 366

MUC 367

MYE 368

MYO 369

Protein Spectra: N 389

NAD 389

NER 392

NEU 393

NIT 395

NUC 399

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xvi Contents

This page has been reformatted by Knovel to provide easier navigation

Protein Spectra: O 403

OLD 403

ORC 404

OVO 405

OXY 408

Protein Spectra: P 409

PAP 409

PAR 411

PEP 412

PER 413

PHA 427

PHE 428

PHO 429

PHY 438

PIG 442

PLA 443

POL 444

PRE 445

PRO 447

PYO 476

PYR 477

Protein Spectra: R 484

RES 484

RET 485

RHO 487

RIB 495

RNA 511

ROD 513

RUB 515

Protein Spectra: S 516

SAL 516

SER 518

SPO 521

STE 522

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Contents xvii

This page has been reformatted by Knovel to provide easier navigation SUB 523

SUC 524

SUP 525

Protein Spectra: T 528

TAU 528

THR 529

THY 532

TOX 533

TPN 535

TRA 536

TRO 540

TRY 541

TUB 551

TYR 552

Protein Spectra: U 554

UME 554

URO 555

Protein Spectra: V 557

VAS 557

VIR 568

Protein Spectra: X 577

XAN 577

General Index 583

Index of Sources 645

Additives and Modifiers which Affect Protein Spectra 674

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NAME: Acetoacetate Decarboxylase SOURCE: Clostridium acetobutylicum

(a bacterium)

REFERENCE: F.Lederer, S.M Coutts, R A

Laursen, and F.H Westheimer, Biochem.,

£, 823 (1966).

EXPERIMENTAL CONDITIONS AND COMMENTS Solvent:

NAME: Acetolactate-forxning Enzyme pH 6

SOURCE: Aerobacter aerogenes (a bacterium)

REFERENCE: F.C Stormer, J Biol Chem ,

2^3, 3IhO (1968).

EXPERIMENTAL CONDITIONS AND COMMENTS

Solvent: 50 mM phosphate, pH 6.0.

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NAME: Aconitase SOURCE: Pig heart REFERENCE: j.j Villafranca and A.S.

Mildvan, J Biol Chem., 2^6, 773

(1971).

Solvent: Curve A: 50 mM Tris-Cl , pH 7.5.

Curve B: Same buffer

REFERENCE: j.i white, H B Bensusan, S.

Himmelfarb, B E Blankenhorn, and W R

Amberson, Am J Physiol., 188, 217 (1957)

Solvent: 0.02 M potassium phosphate with

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NAME: oc-Actinin, 1OS; Or-Actinin, 6S;

NAME: Acyl Carrier Protein

SOURCE: Escherichia coli (a bacterium)

REFERENCE: E L Pugh and S.J Wakil, J Biol.

Chem., 2UO, ^727 (1965)

Solvent: 0.01 M potassium phosphate, pH 7.0.

Protein concentration was 1.2 mg/ml

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NAME: Adenosine Deaminase SOURCE: Calf intestinal mucosa REFERENCE: G Ronca, M F Soettone, and A.

Lucacchini, Biochim Biophys Acta?

NAME: Adenosine Deaminase

SOURCE: Calf intestinal mucosa

REFERENCE: G Ronca, M F Saettone, and A.

Lucacchini, Biochim Biophys Acta, 206,

hlk (1970)

Solvent: 0.1 M sodium phosphate, pH 7.5.

Curve 1: Adenosine deaminase

Curve 2: 39$ Inactivated

Curve 3'- 70$ Inactivated

Curve k: Theoretical spectrum resulting from

addition of adenosine deaminase and9-[p-acetamidobenzyl]adenine

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NAME: Adenosine Deaminase SOURCE: Calf spleen

REFERENCE: N Pfrogner, Arch Biochem.

NAME: Adenosine 5f-Phosphosulfate Reductase

SOURCE: Thiobacillus thioparus (a bacterium)

REFERENCE: R M Lyric and I Suzuki, Can J.

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NAME: Adenosylmethionine Decarboxylase

SOURCE: Escherichia coli W (a bacterium) REFERENCE: R B Wickner, C W Tabor, and

H Tabor, J Biol Chem., 2^5., 2132(1970)

Solvent: 0.05 M potassium chloride w ith

10 mM potassium phosphate, pH 6.35,

1 mM EDTA, and 1 mM 2-mercaptoethanol.Protein concentration was 1.35 mg/ml

NAME: Adrenodoxin

SOURCE: Pig adrenal glands

REFERENCE: T Kimura, in Biological and

Chem-ical Aspects of Oxygenases (K Bloch and

O Hayaishi, eds.), Maruzen Co Ltd 1966

Solvent: 0.01 M phosphate buffer, pH l.h.

100 muatoms of iron per ml

,Enzyme Phenylhydrazone

Enzyme alone

Pyruvate Phenylhydrazone

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NAME: Alanine Dehydrogenase SOURCE: Bacillus subtilis (a bacterium) REFERENCE: J.M Lebeault, C Zevaco, and

J Hermier, Bull Soc Chim Biol.,52., 1073 (1970)

EXPERIMENTAL CONDITIONS AND COMMENTS Solvent: 0.05 M Tris-HCl, pH 8.0.

Protein concentration was 0.088 mg/ml

NAME: Albocuprein I

Albocuprein II

SOURCE: Human brain

REFERENCE: H Fushimi, C R Hamison, and H.A.

Ravin, J Biochem , Tokyo, (Q , 10^1 (1971)

Solvent: 0.05 M acetate buffer, pH 6.0.

: Albocuprein I, 10.03 mg/ml invisible and 0.3^ mg/ml in ultra-violet regions

: Albocuprein II, 7 » 6 2 mg/ml invisible and 0.51 mg/ml in ultra-violet regions

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NAME: Albumin SOURCE: Bovine serum REFERENCE: F Chu, Arch Biochem Biophys.,

NAME: Albumin : Ochratoxin Complex

SOURCE: Bovine serum

REFERENCE: y% Chu, Arch Biochem Biophys.,

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NAME: Albumin SOURCE: Beef serum REFERENCE: R Koberstein, B Weber, and

R Jaenicke, Zeit Naturforsch., 23b,

Curve k: 2-1, O hours.

Curve 5: 2-1, H hours daylight

Curve 6: 2-1, 10 hours daylight

NAME: Albumin

SOURCE: Beef serum

REFERENCE: R- Koberstein, B Weber, and R.

Jaenicke, Zeit Waturforsch., 23b, kfk

(1968)

S o l v e n t : : p H 2

: PH : pH 9-Curve 1: Albumin vs buffer

7-Curve 2: Actinomycin C vs buffer

Curve 3: Albumin + Actinomycin C vs

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NAME: Albumin SOURCE: Bovine serum REFERENCE: L Jirousek and E.T Pritchard,

Biochim; Biophys Acta, 229> 6l8

(1971)-EXPERIMENTAL CONDITIONS AND COMMENTS

Solvent: 0.1 M sodium phosphate buffer,

pH h.5.

Curve 1: 0.2 UUK)Ie albumin in 2.2 ml.Curve 2: 0.2 umole iodine added

Curve 3: 0.3 umole iodine added

Curve h: O.k umole iodine added.

Curve 7« 1-0 umole iodine added

Curve 9: l.U umole iodine added.

Curves not corrected for volume changes

1 mM aqueous iodine used, T = 50C

NAME: Albumin sulfenyl iodide

3-Lactoglobulin sulfenyl iodide

Bovine milk

REFERENCE: L Jirousek and E.T Pritchard,

Biochim Biophys Acta, 229, 6l8 (1971)

Solvent: Water: Curves 3 and U.

pH U 5: Curve 7

pH 6.1: Curves 1,2 and 6

pH 7.!*: Curve 5

Curve 1: 0.2 umole 3-lactoglobulin + 0.2

umole Iodine in 2.2 ml buffer

Curve 2: 0.2 umole albumin + 0.2 umole

iodine in 2.2 ml buffer

Curve 3: 0.6 umole iodine in 2.8 ml water

Curve k: 0.19 umole !3 in 2.25 ml water.

Curve 5: 0.2 umole albumin +0.5 umole

iodine in 2.9 ml buffer

Curve 6: 0.2 umole P-lactoglobulin + O.l6

umole IJ in 0.2 M KI

Curve 7: 0.2 umole (3-lactoglobulin +0.6

umole iodine in 2.U ml buffer

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NAME: Albumin SOURCE: Bovine serum REFERENCE: I SeIa and Y Antignus, Anal.

Curve e: Albumin, 20 ug/ml

Curve f : TMV coat protein, 20 ug/ml

NAME: Albumin,

Cupric-Hemocyanin

Busycon canaliculatum (a snail)

REFERENCE: I.M Klotz and T.A Klotz, Science,

Trang 25

NAME: Albumin SOURCE: Bovine serum REFERENCE: G C Webster, Biochim Biophys.

REFERENCE: W.F Goebel and G E Perlmann, J.

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NAME: Albumin SOURCE: Bovine serum REFERENCE: B.D Polis, J Wyeth, L.

Goldstein, and J Graedon, Proc Nat.Acad S c i * 6A, 755 (1969)

Solvent: 0.1 M KCl-0.05 M phosphate buffer,

PH 7-0.

: Normal serum albumin.

: Albumin free radical.

: Difference spectrum.

Concentration: 1 gm/1.

NAME: Albumin

Nitroguanyl-albumin

REFERENCE: A F S A Habeeb, Biochim Biophys.

Trang 27

NAME: Albumin SOURCE: Bovine serum REFERENCE: E K Rideal and R Roberts, Proc.

Roy Soc London, 205A, 391 (1951)

: Theoretical curve

: Experimental curve

NAME: Albumin

REFERENCE: R.T Taylor and M.L Hanna, Arch.

Biochem Biophys., lUl, 2^7 (1970)

Solvent: 20 mM KCN + 20 mM NaOH.

AgUO-B12-BSA complex 60 minutes after

alkaline-KCN treatment at 220C;

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NAME: Albumin SOURCE: Bovine serum REFERENCE: R T Taylor and M.L Hanna,

Arch Biochem Biophys., lUl, 2kj (1970).

EXPERIMENTAL CONDITIONS AND COMMENTS Solvent: KH2PO]1 buffer, 50 mM

A Curve 1: AqUO-B12*Curve 2: Cyano- B^2.Curve 3: Aquo~B-j_2-albumin complex,

REFERENCE: R T Taylor and M L Hanna, Arch.

Biochem Biophys., lUl, 2^7 (1970)

Solvent: KH2POj4 buffer, 50 mM

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NAME: Albumin, and glutaraldehyde-treated

pH at which the reaction was run

a , b , c , indicate time of reaction, 1/2

hr, 1 hr, and 2 hr

NAME: Albumin

REFERENCE: C.M King and E Kriek, Biochim.

Biophys Acta, 111, 1^7 (1965)

Solvent: 0.1 M sodium phosphate buffer, pH 7.U.

: Albumin, 10 mg/10 ml

: Albumin-3-hydroxyanthranilic acid

add uc t

: Albumin-2-aminophenol adduct

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NAME: Albumin SOURCE: Bovine serum REFERENCE: G H Beaven and E R Holiday,

Adv Prot Chem , £, 319 (1952)

Solvent: Curves 1 and 2: Acid.

Curves 3 and h: Alkali Curves 2 and h before peptic digestion.

Curves 1 and 3 after peptic digestion

NAME: Albumin-Cu(ll) Complex

SOURCE: Human serum

Dog serum

REFERENCE: D W Appleton and B.Sarkar, J Biol.

Chem., 246, 50^0 (1971)

Solvent: Buffers of different pH.

A Human Serum Albumin

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NAME: Albumin-Cu(II) + 1 eg C u ( I l ) SOURCE: Human serum

Solvent: 0.01 M phosphate buffer, pH 7.0.

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NAME: Albumin SOURCE: Human serum REFERENCE: W Katz, K M Larrson, and T H

Mead, J Gen Virol , 2., 399 (1968)

EXPERIMENTAL CONDITIONS AND COMMENTS Solvent: 0.02 M phosphate buffer, pH 7 - 8

SOURCE: Human serum

REFERENCE: W L Hughes, Jr and R Straessle,

J Am Chem Soc , 72., ^52 (1950)

Solvent: pH

10.75-Curve O Albumin

Curve 7 7 atoms of iodine/mole protein

Curve I^ ±h atoms of iodine/mole protein.

Curve 29 29 atoms of iodine/mole protein

Curve 3^ 3^ atoms of iodine/mole protein

Curve 6l 6l atoms of iodine/mole protein

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NAME: Albuminoid SOURCE: Eye lens REFERENCE: C.R Hamlin, Exp Gerontol., ^,

Curve B: Absorption spectrum after

correction for scattering

NAME: Alcohol Dehydrogenase

SOURCE: Liver

REFERENCE: C Woenckhaus and R Jeck,

Hoppe-Seyler's Z Physiol Chem., 352, IUlT

(1972)

Solvent: 0 , 2 M phosphate b u f f e r , pH 6 5

-Alcohol inactivated enzyme

U.2 mg/ml enzyme; 3 hours afteraddition of 10 umoles acetaldehyde

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NAME: Alcohol Dehydrogenase SOURCE: Yeast

REFERENCE: E S Guzman Barron and S Levine,

Arch Biochem Biophys., JU9 175 (1952)

Solvent: 0.01 M pyrophosphate buffer

pH 8.8, 250C

OCurve 1: DPNH, 2.7 x 10 M

-9Curve 2: Protein, 3.1 x 10 M

Curve 3: Protein + DPNH

NAME: Aldehyde Oxidase

SOURCE: Rabbit liver

REFERENCE: K V Rajagopalan and P Handler,

J Biol Chem., 239, 1509 (196*0

Solvent:

Top curve: Oxidized enzyme

Bottom curve: Equivalent amount of FAD

Middle curve: Enzyme spectrum minus flavin

spectrum

Trang 35

NAME: Aldehyde Oxidase, flavin free SOURCE: Rabbit Liver

REFERENCE: K.V Rajagopalan and P Handler,

J Biol Chem., 239, 1509 (1964)

Curve 1: Oxidized protein

Curve 2: Reduced with dithionite

SOURCE: Rabbit liver

REFERENCE: K V Rajagopalan and P Handler,

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NAME: Aldehyde Oxidase SOURCE: Rabbit liver REFERENCE: K V Rajagopalan and P Handler,

J Biol Chem., 239, 1509 (196U)

Top curve: Oxidized enzyme

Bottom curve: Reduced with dithionite.Intermediate curves: Increasing amounts

of N-methylnicotinamide at 250C

SOURCE: Pig liver

REFERENCE: H R Mahler, B Mackler, D E

Green, and R.M Bock., J Biol Chem.,

210, U65

(195*0-EXPERIMENTAL CONDITIONS AND COMMENTS

Solvent:

Upper curve: oxidized enzyme

Lower curve: Reduced enzyme:

1.12$ solution of enzyme

Enzyme reduced with 10 pM acetaldehyde

OXIDIZED

REDUCED

Trang 37

NAME: Aldolase, Azo- , Chymotrypsin, Azo- ,

Elastase, AZO-, and y-Globulin,

Curve C : Azo-Aldolase (Rabbit)

Curve D: Azo- y-Globulin (Bovine).Proteins treated with diazotizedp-arsanilic acid for 30 minutes at

Trang 38

NAME: Aldolase, cobalt containing SOURCE: Saccharomyces cerevisiae ( a yeast) REFERENCE: R T Simpson, R D Kobes, R W

Erhe, W J Rutter, and B.L Vallee,Biochemistry, 10, 2^66 (1971)

: Aldolase cobalt containing.: 0.01 M fructose 1,6-diphosphateadded

NAME: Aldolase, cobalt containing

SOURCE: Saccharomyces cerevisiae (a yeast)

REFERENCE: R T Simpson, R D Kobes, R W

Erbe, W J Rutter, and B L Vallee,

Trang 39

NAME: Aldolase SOURCE: Boa constrictor constrictors (snake) REFERENCE: E Schwartz and B.L Horecker,

Arch Biochem Biophys., 115, ^07(1966)

EXPERIMENTAL CONDITIONS AND COMMENTS Solvent: 0.05 M Tris-HCl buffer, pH 7-3.

Aldolase at pH 7 3 Acid (pH 2 U ) dissociatedand then brought to pH 7 « 3

-NAME: Allergens

SOURCE: Varied

REFERENCE: L Berrens and E Bleumink, Int.

Arch Allergy, 28, 150 (1965)

Solvent: Q Ol M phosphate buffer, pH 7-0.

Curve A: Liquorice allergen.

Curve B: Tomato allergen.

Curve C: House dust allergen.

Curve D: Ipecac allergen.

Curve E: Human dandruff allergen.

Curve F: Horse dandruff allergen.

Curve G: Trichophytin.

Curve H: Cottonseed allergen.

ABSOPBANCY

WAV£L€HGrH,

Trang 40

NAME: Amine Dehydrogenase, derivatives

SOURCE: Pseudomonas AMI (a bacterium) REFERENCE: R R Eady and P.J Large,

NAME: Aniine Dehydrogenase , methylamine

SOURCE: Pseudomonas AMI (.a bacterium)

REFERENCE: R R Eady and P.J Large,

Biochem J , 123, 757

(1971)-EXPERIMENTAL CONDITIONS AND COMMENTS

Solvent: 5 mM phosphate buffer, pH 7.5.

Curve a: Methylamine-treated enzyme

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